Molecular Biotechnology

• Understanding the importance of biotechnology

• Onboarding

• Motivation and goal setting

• Building a strong foundation in key skills

• Career exploration and networking

• Ethical considerations and emerging trends

• Part of a wBecoming part of a community of practice

Lecture, individual and group work, practical implementation tasks, self-assessment through exercises for self-reflection and individual application, practical exercises with feedback and analysis

Continuous assessment: Performance assessment (e.g. presentation, discussion, written work, reflection)

• The Austrian Federal Constitution at a glance

• The administration

• Federalism and the European Union

• Trade law

• Reproductive medicine law

• Genetic engineering law

• Animal welfare law

• pharmaceutical law

In the general part of public law, students acquire basic knowledge of the fundamental principles of Austrian constitutional law, the structure of legislation, the types and principles of enforcement and the various possibilities of legal protection.

They deal intensively with the legal basis for the commencement, exercise and termination of a commercial activity. Topics such as the classification of trades, the requirements for exercising a trade (e.g. capacity to act under trade law, certificate of competence), the scope and loss of trade licenses and the role of tradespeople are covered. A special focus is placed on the law on business premises, including the definition of commercial business premises and licensing requirements.

Another focus is the topic of "biomedicine". Students analyze constitutional and statutory provisions of reproductive medicine law, organ transplantation law and the protection of life and discuss these in the context of ethical issues.

In the area of animal protection law, animal experimentation law and the central regulations of the Animal Protection Act are explained. In addition, students acquire knowledge of the main features of genetic engineering law, including regulations for work in closed systems, safety requirements and regulations on the release and marketing of genetically modified organisms (GMOs).

Presenting method

Final exam: Written final exam

The focus is on supporting students in their presentation confidence and self-organization and preparing them for presentation and discussion situations in everyday working life. In the first semester, presentation confidence and presentation techniques are trained and consolidated. The teaching objectives include refreshing, consolidating and deepening basic presentation skills. The main topics are authenticity, dramaturgy and differentiating between scientific and persuasive presentations. Personal style and goal-oriented presentation are continuously developed through implementation exercises with intensive feedback.

Lecture, individual and group work, practical implementation tasks, self-assessment through exercises for self-reflection and individual application, practical exercises with feedback and analysis

Continuous assessment: Performance and progress are assessed on an ongoing basis. The assessment is based on all written and oral work during the semester. Collaboration is also taken into account.

This lecture deals with the theoretical principles of wet chemical analysis of inorganic and organic samples. The focus is on preliminary samples and individual detections of anions, cations and inorganic salts, with particular attention to the specificity of the detection reactions, reaction equations and stoichiometry. Video visualizations clearly convey laboratory practice and prepare students for practical implementation. In addition, basic analysis methods for organic samples are developed. These include detection methods for functional groups as well as simple extraction and separation techniques, which are illustrated using selected organic compounds. In addition, the basic principles of wet-chemical quantitative analysis techniques are discussed. The aim of the course is to create a solid analytical basis for practical laboratory work.

Presentational method, lecture with interactive intermediate exercises

Final exam: Final written examination

The laboratory training program is divided into several modules that build on each other and promote practice-oriented work and independent learning:

1. Fundamentals of laboratory technology/safety: introduction to basic chemical working techniques and elementary safety rules in the laboratory.

1. Qualitative analysis of liquid mixtures: Separation and qualitative analysis of inorganic anion and cation mixtures using wet-chemical analytical methods.

1. Qualitative analysis of solids: Identification of inorganic and organic salts based on previously acquired knowledge.

1. Quantitative analysis: Determination of content by dimensional analysis.

Record keeping:
The test results are documented by hand, focusing on a structured and precise presentation of the work processes and results.

Mainly working methods

Final exam: Final examination, immanent examination character

Atomic structure: Structure of the atom, elementary particles, elements; isotopes; radioactive decay, (radioactive) displacement theorems, decay series.

Atomic models: Rutherford model, Bohr model, wave mechanical model.

Periodic table of the elements: periods and groups, main group elements and subgroup elements, electron configuration of the elements, general relationships of the periodic table.

Bonds (with special consideration of the resulting spatial structure): Metal bonding, Ionic bonding, Covalent bonding, Coordinative bonding; Intermolecular bonding forces; Acid-base concept.

Conservation laws and consequences: stoichiometry, energy and enthalpy, entropy, spontaneity of chemical reactions, redox reactions.

State forms of matter and their laws.

Chemical equilibrium, law of mass action, acids/bases in detail, pH value.

Lecture with active involvement of the students, homework for self-training of presented concepts

Final exam: Written final exam

Based on the question: "What is life?", physical laws and chemistry as the basis for life (biomolecules, energy production, metabolism, respiration, photosynthesis) are discussed first. Biomolecules such as proteins are discussed in detail. This is followed by Darwinian evolution, forces and mechanisms of evolution, speciation and the origin of life. Hierarchy of life, kinship of organisms, sequence comparisons at DNA and protein level. Milestones in the history of life on our planet are discussed, as well as the origin of eukaryotic cells and multicellular organisms.

Presenting method

Final exam: Written final exam on the computer (multiple choice)

• Cells as the basic building blocks of life

• Common characteristics of cells

• Characteristics of prokaryotes and eukaryotes

• Presentation of simple microscopy specimens (prokaryotes, eukaryotes)

• Cells in selected animal tissues and plants

• Selected areas of plant anatomy

• Microscopic techniques

• Fluorescence microscopy

• Electron microscopy

Presenting method, lecture with activating methods

Final exam: Written final exam

The lecture includes the following topics:
(1) Introduction to microbiology (definition of microorganisms; history of microbiology; influence of microorganisms)

(2) Microbial evolution and diversity (origin of life; phylogenetic tree of life; methods for determining evolutionary relationships; microbial diversity)

(3) Structure and function of microbial cells (overview and differences between prokaryotic and eukaryotic cells)

(4) Microorganisms and their natural environment (nutrients; environmental factors; habitats)

(5) Microbial metabolism

(6) Cultivation and growth of microorganisms

(7) Control of microbial growth (in vitro and in vivo applications)

(8) Interactions between microbes and humans (beneficial and harmful)

(9) Introduction to medical microbiology (epidemiology; microbial diseases; diagnostic microbiology.

The content of the lecture is taught using a Power Point presentation as part of frontal teaching.

Students always have the opportunity to ask questions during the course, which may be discussed with the plenum.
At the end of each chapter, the most important key messages of the topics presented are summarized in the form of take home messages and questions related to the topics covered in the teaching unit are presented, which are similar to the type of exam questions.

In addition, on selected days at the beginning of a teaching unit, students' learning progress is checked in the form of a quiz.

Some teaching units of the course are designed as distance learning. Here, students are asked to read articles on the subject of microbiology, the content of which is then also tested in the final examination.

Final exam: Final written examination at the end of the course

• Cooling the microscope and calibrating the measuring eyepiece
• Carrying out a plasmolysis (e.g. onion) and microscopic evaluation
• Staining and analysis for starch detection (e.g. potato, banana, wheat)
• Staining and analysis of cells of the oral mucosa
• Microscopic analysis of pond water
• Preparation and microscopy of chromoplasts in plant tissue (e.g. carrot)
• Preparation and microscopy of the plant cell wall (lignified, non-lignified; with staining)
• Preparation and microscopy of a leaf cross-section
• Microscopy of a human hair, as well as finished preparations (blood smear, mitosis stages of an onion, skin preparations, etc)

Documentation of all microscopic analyses and measurements using a measuring eyepiece or camera.

Practical course, classroom teaching (preliminary discussion), distance learning

Continuous assessment: The overall grade results from the commitment during the internship, the assessment of the quality of the protocols to be prepared during the internship, as well as the submission of a work assignment.

The Molecular Biology and Genetics I course covers a wide range of fundamental topics in genetics and molecular biology. The course begins with an introduction to the field, including its history and relationship to other disciplines such as biochemistry and cell biology. The course also covers important discoveries that have expanded our understanding of the interactions of DNA, RNA and proteins. Students will learn about Mendelian inheritance, including the concepts of dominant and recessive alleles, segregation, and independent assortment. Building on this foundation, the course examines the central dogma of molecular biology that explains the flow of genetic information from DNA to RNA to proteins. Students gain an in-depth understanding of DNA replication, including the role of key enzymes and the challenges of end replication. The course then compares and contrasts DNA and RNA and examines different types of RNA and their functions. Students will learn about the structure of the genome, how DNA is packaged into chromosomes, and the different types of chromatin. The course also covers DNA mutations and repair mechanisms, including different types of mutations and how cells correct errors in DNA. Finally, the course covers homologous recombination, site-specific recombination, transposable elements and V(D)J recombination.

Presenting method with instructional videos

Final exam: Written final exam

Solutions: Concentration specifications, preparation of solutions and solution mixtures

pH value: acidic/basic solutions, buffer solutions

Quantitative analysis: From measured value to content specification - using the example of: Gravimetry, titration, photometry, chromatography

• Accuracy, correctness, precision, detection limit, limit of quantification

• Errors

• Calibration / Adjustment

• Evaluation and documentation of analysis results

The basic calculation operations are presented and discussed in detail using selected practical examples. A specific e-learning tool is provided for personal calculation training.

Lecture with active involvement of the students

Homework and exercises (with e-learning tool "Chemical Calculation")

Final exam: Written final exam

Spatial and temporal homogeneity of exponential growth and decay.

Linear recursions, real and complex eigenvalue analysis, in this context calculations with vectors, matrices and determinants, solution methods of linear equation systems.

Concrete models from population dynamics: Leslie, Levkovich and predator-prey models.

Complementary to the solution behavior of linear recursions, the logistic growth equation, Cobweb and bifurcation diagrams.

Integrated online course

Continuous assessment: Immanent examination character. The course is assessed by regular short intermediate examinations and a final semester project. These are written. Possible questions are clarified in oral form.

• Basic concepts of ethics
•  Ethical theories
• Ethics in decision-making and reflection models
• Ethics in everyday life - personal and professional responsibility
• Insights into the ethics committee at FH Campus Wien
• New development trends and their ethical relevance 
• Ethical issues in relation to the professional field
•  current topics in (bio)ethics

Lecture with activating methods, group work, discussion, work assignments with (peer) feedback, presentation, reflection, blended learning

Continuous assessment: Immanent performance review

You will learn the basics of self-coaching and stress management techniques and become aware of personal perception and communication patterns. Methods of self-motivation, time management and stress reduction are tried out and reflected upon, and the effects of perception on behavior and communication are analyzed. In addition, practical experience in self-management for later professional life is gained through implementation tasks. Key topics are self-coaching and communication, self-coaching and self-motivation, stress and time management, perception and interpretation, communication analysis

Lecture, individual and group work, practical implementation tasks, self-assessment through exercises for self-reflection and individual application, practical exercises with feedback and analysis

Continuous assessment: Performance and progress are assessed on an ongoing basis. The assessment is based on all written and oral work during the semester. Collaboration is also taken into account

Students are taught the physical, chemical and cellular principles of the composition and molecular structure of biomacromolecules (proteins, nucleic acids, polysaccharides and lipids). A special focus is placed on the importance of carbon for the chemistry of living organisms and on the important role of water for the structure and function of biomacromolecules. Amino acids and proteins, sugars and polysaccharides, as well as fatty acids and lipids are then examined in more detail. The chemistry of the covalently linked monomers (amino acids, monosaccharides, fatty acids) is always considered first and then the structure of the macromolecules and supramolecular complexes is described. Particular emphasis is placed on the following points: 1) that the unique structure of macromolecules determines their function, 2) that non-covalent interactions play a crucial role in the structure and function of macromolecules and 3) that monomers of polymeric macromolecules have a specific order that provides information on which the ordered state of life depends.

Presenting method

Final exam: Written final exam, essay questions

1. atomic orbitals - hybridization of alkanes, alkenes and alkynes

2. bond types: Covalent bonding, Π-bonding, van der Waals bonding, hydrogen bonding

3. mesomers and inductive effects

4. classes of substances: Saturated and unsaturated hydrocarbons, aromatic compounds, haloalkanes, alcohols, phenols, ethers, sulphur compounds, aldehydes, ketones, carboxylic acids and derivatives, carbonic acid and derivatives, amines; trivial nomenclature of important alcohols, phenols, aldehydes, ketones, carboxylic acids, amines, etc.

5. oxidations, reductions

6. stereoisomerism - mirror image isomerism: constitution, configuration, conformation; chirality, enantiomers, diastereomers, racemate cleavage of acidic or basic compounds; polarimetry, determination of optical purity

7. acid/base strength of organic compounds

8. reaction mechanisms: Nucleophilic substitution reactions on the total C atom, electrophilic substitution reactions on aromatic compounds, electrophilic and nucleophilic additions to C,C double bonds, condensations on the carbonyl group: acetals, cyanohydrins, reductions with sodium borohydride and lithium aluminum hydride, Grignard reactions, aldol and Knoevenagel condensations, Wittig and Mannich reactions, addition/elimination reactions on the carboxyl group, eliminations

Presenting method

Final exam: Written, LV-related questions

Tasks of quantitative analysis and their basic measuring instruments (volumetric instruments and balances). Preparation of solutions taking stoichiometry into account. Methods of dimensional analysis (acid-base and redox titrations) including content determination. Instrumental methods for the qualitative and quantitative determination of organic molecules (photometry, chromatography) as well as potentiometric methods (pH value, ion-selective electrodes) for the analysis of ions.

Performing & activating methods

Final exam: Written final exam

The laboratory exercise includes the detection of covalently bound elements such as nitrogen, sulphur, halogen and others. Thermal analyses are also carried out. Refractometry is used to determine the refractive index of a pure liquid and the concentration of a sucrose solution. Photometry is used to determine the concentration of a compound (recording and interpretation of a UV spectrum/ calibration curve). The program also includes two potentiometric examples for quantitative determination. Another important part of the laboratory exercise is devoted to chromatography. Column chromatography is introduced. Drugs (sulfonamides, barbiturates) are identified using thin-layer chromatography. A mixture of organic molecules is also analyzed qualitatively and quantitatively using high-performance liquid chromatography. Method validation is used in this context. Type of protocol: Results protocol to be filled out.

Practical implementation in the laboratory, activating methods, e-learning

Final exam: Verification through assessment of the analysis results

The lecture "Gene Expression", provides a detailed presentation of gene expression, including the processes of transcription and translation and their regulation. The course emphasizes the importance of model organisms such as E. coli, yeast and Drosophila for understanding these fundamental concepts. Beginning with an examination of transcription, the course covers the roles of RNA polymerases, promoters, and the three phases of transcription: initiation, elongation, and termination. It then moves on to RNA splicing, emphasizing the function of the spliceosome in removing introns and the effects of alternative splicing in generating different protein isoforms. The translation process is explained, focusing on ribosomes, tRNAs and the intricate mechanisms of polypeptide chain synthesis. The genetic code is also discussed, including its properties such as degeneracy and universality, and the effects of mutations on the coding sequence. Regulation of gene expression is another central theme of the course, covering both prokaryotic and eukaryotic mechanisms. The course also discusses the role of regulatory proteins, enhancers, silencers and chromatin remodeling in the control of transcription. The course also introduces the concept of regulatory RNAs such as siRNAs and miRNAs and their effects on gene expression. Finally, the course provides a practical perspective by covering basic molecular biology methods, including PCR, sequencing and protein analysis techniques.

Presenting method with instructional videos

Final exam: Written final exam

This lecture in the Bachelor's degree course in Molecular Biotechnology summarizes the most important principles and techniques of recombinant DNA technology. Biotechnology utilizes living organisms or their products for the benefit of humans, with modern applications ranging from antibiotic production to genome sequencing. A cornerstone of biotechnology is recombinant DNA technology, which enables the manipulation and creation of novel DNA combinations. This field relies heavily on gene cloning, a process that involves multiple steps including gene isolation, vector selection, restriction digestion, ligation, transformation and screening to generate numerous copies of a given gene. Plasmids, circular DNA molecules, serve as common vectors to carry the gene of interest. These vectors have an origin of replication (ori), a selectable marker (often an antibiotic resistance gene) and a multiple cloning site (MCS) for the insertion of foreign DNA. The essential enzymes for working with recombinant DNA include restriction enzymes for DNA cutting, ligases for joining DNA fragments and polymerases for DNA synthesis. Transformation, i.e. the introduction of plasmid DNA into bacterial cells, can be achieved by methods such as heat shock or electroporation. In addition to the cloning of genes, the lecture examines the expression of proteins from cloned genes using special expression vectors. These vectors use specific promoters to control gene expression and can contain markers for protein purification and identification. The lecture also discusses advanced cloning techniques such as PCR cloning and Gibson assembly. Cosmids, bacterial artificial chromosomes (BACs) and yeast artificial chromosomes (YACs) will also be discussed.

Presenting method with instructional videos

Final exam: Written final examination

Simple models from population dynamics, population genetics and epidemiology are discussed.

(1) Leslie models of real populations based on empirically measured rates,

(2) Population genetics: Hardy-Weinberg equilibrium of large ensemble populations.

In contrast

(3) Small ensemble populations based on the Fisher-Wright model.

Integrated online course

Final exam: The course is assessed on the basis of regular short exercise tests, an ongoing exercise group project and a written examination at the end of the course. Possible questions will be clarified orally.

Fundamentals of probability theory and statistics with a focus on applications in biology.

(1) Descriptive statistics:

Elementary description and visualization of random samples using GNU R software.

(2) Probability theory:

Calculating with probabilities, Bayes' theorem.

(3) Probability theory:

Random variables, simple stochastic processes.

(4) Inductive statistics:

Parameter estimation, confidence intervals, hypothesis testing.

(5) Reproducible Research

Basics in the automated generation of statistical reports.

Integrated online course

Final exam: The course is assessed by a combination of regular short exercise tests, ongoing exercise projects and a written examination at the end of the course. Possible further questions on the projects can also be clarified orally.

The Applied Microbiology course deals with the practical and theoretical principles of handling microorganisms and their diverse applications in research, industry and medicine. The initial focus is on safe and sterile work in the microbiology laboratory, i.e. the correct handling of potentially pathogenic microorganisms, compliance with safety standards and the avoidance of contamination. Building on this, students learn methods for the enrichment, cultivation, storage and identification of microorganisms. Microbial growth and its measurement are also discussed.

Furthermore, the course teaches the basics of bioprocess engineering. This knowledge is directly linked to practical applications, such as food fermentation (e.g. in the production of bread, beer, yoghurt or cheese).

The medical dimension is also covered: Students deal with the mechanisms of action of antibiotics, the resistance strategies of microorganisms and their significance for medicine. They also learn about test methods that can be used to test the effectiveness of antibiotics. The biotechnological production of pharmaceutical proteins such as insulin or antibodies is also discussed.

Finally, the course promotes the ability to deal with current scientific publications, to discuss them critically and to summarize them concisely.

Lecture, presentation method, activating methods (quizzes, exercises), distance learning (paper revision), group discussions

Final exam: The overall grade is made up as follows:

80% final written examination

20% written work (paper revision)

This lecture provides an introduction to the subject of virology. The most important characteristics of viruses are explained to the students and they are given an understanding of virus classification. In addition, students learn about important representatives of bacteriophages and important human pathogenic viruses and gain an insight into virus-cell interaction and virus-virus interactions. Furthermore, basic principles of virus structure, viral genome organization, viral replication and gene expression are discussed and the life cycles of some selected viruses are compared. In addition, similarities and differences between viruses and subviral particles are also discussed.

Presenting method

Final exam: Written final exam, multiple choice part, essay questions

The course aims to provide students on the Bachelor of Molecular Biotechnology program with a comprehensive understanding of the structure and function of eukaryotic cells. The course introduces eukaryotic cells and examines macromolecules such as proteins and lipids. It also covers membranes and transport processes, organelles and vesicle transport, the cytoskeleton and cell movement, and energy production in mitochondria and chloroplasts. The cell is the smallest living unit that is enclosed by a membrane and can replicate itself. Eukaryotic cells differ from prokaryotes by the presence of a nucleus, which stores genetic information. Cell biology studies the complex processes of the cell, covering a wide range of vital processes. Microscopy plays a crucial role in the visualization and examination of cells. Biological membranes, which consist of phospholipid bilayers, regulate the passage of molecules in and out of the cell and its organelles. Nerve conduction is based on the transmission of electrical signals (action potentials) along the neurons. Intracellular transport involves the movement of molecules and organelles within the cell, which is facilitated by the cytoskeleton. The cytoskeleton provides structural support and facilitates cell movement. It consists of intermediate filaments, microtubules and actin filaments. Energy production in mitochondria (oxidative phosphorylation) and chloroplasts (photosynthesis) utilizes energy from the electron transport chain to generate ATP. Cell-cell junctions maintain tissue integrity and enable communication between cells. This course provides students with a foundation in eukaryotic cell biology that is essential for further study and research in molecular biotechnology.

Presenting method with instructional videos

Final exam: Written final exam

1. historical development and current tasks of common quality management systems

2. overview of quality management systems (especially TQM, ISO 900x, ISO 17025)

3. overview of relevant legal background (especially GLP, GMP, basic GCP, accreditation, notified bodies, EU market surveillance / new approach)

4. definition, meaning and content of

i) Quality

ii) Quality management,

iii) Quality management system (QM system),

iv) The quality cycle: quality planning, control, assurance, inspection, improvement,

v) Quality audit

5) Product quality, process quality

6) Benchmarking

7) Process management: process definitions, key figures

8. processes in the company

i) Core processes (value creation)

ii) Management processes

iii) Supporting processes

9. processes and management systems

10. measurement and control of processes

11. processes and change

Presenting method

Final exam: Final exam: Moodle final exam

Introduction to the different subject areas of bioinformatics:

• Basics of sequence analysis, in particular transcript and genome analysis

• Relationship between sequence, structure and function of proteins

• Metabolic models

• Phylogenetic studies

• Metagenome analyses

• Presentation of the most important relevant databases

Practical experience: Practical examples of the topics covered in theory, use of the relevant databases, sequence comparisons, gene expression analysis in R. Introductory programming examples.

Performing & activating methods

Final exam: Working on examples and self-test with Moodle

Poisson processes

Fluctuation test according to Luria-Delbrück

Classical parameter and distribution tests

Linear regression

One-factor analysis of variance

Integrated online course

Final exam: Immanent examination character. The course is assessed by regular short intermediate examinations and a final semester project. These are written. Possible questions are clarified in oral form.

Thermodynamics and kinetics of protein folding: Anfinsen experiment, Levinthal paradox, classical folding models and "new view" folding funnels. Role of molecular chaperones in in vivo protein folding. Metamorphic and intrinsically disordered proteins and their role. Protein folding diseases with a focus on Alzheimer's disease. Brief insight into the pathophysiological phase separation of biomacromolecules. Protein purification and detection methods. Basics of structural elucidation of biomacromolecules using X-ray structure analysis, nuclear magnetic resonance spectroscopy and cryo-electron microscopy. Models of ligand binding (induced fit, lock-and-key, conformational selection/population shift) and their quantitative description using binding isotherms. Principles of allostery and cooperative ligand binding using hemoglobin as an example: MWC and KNF model, Hill diagram. Hemoglobinopathies with a focus on sickle cell anemia. Brief introduction to chemical reaction kinetics. General mode of action of enzymes based on energy profiles and strategies for reducing activation energy. Role of cofactors. Enzyme main classes, enzyme kinetics (Lineweaver-Burk diagram, kinetic parameters (Km, change number, catalytic specificity)). Types and mode of action of enzymatic inhibitors, reaction mechanisms of selected enzymes, reasons for substrate specificity.

Presenting method

Final exam: Written final exam

Introduction to the basics of physical chemistry, first and second law of thermodynamics, enthalpy, entropy, free enthalpy, spontaneous and non-spontaneous processes, driving force of chemical reactions, phase equilibria, phase diagrams, equilibrium reactions, electrochemistry.

Presenting method

Final exam: Written final exam

First, the innate immune system with its characteristic features is described and contrasted with the adaptive immune system. The most important interface between the innate and adaptive immune system, antigen presentation, is then presented. This is followed by a discussion of the development and function of the adaptive immune system.

Presenting method

Final exam: Written final exam

1) General principles of cell and tissue culture (legal principles, guidelines for working in laboratories of safety classes 1 and 2 (S1, S2 laboratories), spatial and instrumental equipment, sterile technology, contamination and how to avoid it)

2) The cell and its environment (culture vessels and their treatment, growth conditions)

3) Routine methods for general handling of cultured cells (medium change, subcultivation, determination of general growth parameters, freezing, storage and shipping of cells)

4) Cell lines versus primary cells (derivation of primary cells, establishment and characterization of cell lines)

5) Cells as factories (hybridoma technology for the production of monoclonal antibodies, production of recombinant proteins, transfection, mass cell cultures)

6) Methods in cell culture

7) Basics of stem cells and plant cell cultures

Presenting method

Final exam: Moodle quizzes, written final exam

The course "Introduction to Molecular Biology Techniques", introduces students to basic molecular biology techniques. It covers restriction enzyme digestion, agarose gel electrophoresis and DNA concentration determination by spectrophotometry. Students will gain hands-on experience in performing these techniques, analyzing experimental data, and creating a restriction map of an unknown plasmid. The course emphasizes safe laboratory practices, including enzyme handling, waste disposal, and proper pipetting techniques using automated pipettes. Furthermore, results are recorded in the form of a scientific lap report in English.

Activating methods

Final exam: Protocol in English, cooperation

In this practical course, a gene is inserted into a plasmid and various molecular methods (PCR, restriction digestion) are then used to check whether the recombinant plasmid is stable in E. coli. Before starting the practical course, the students prepare in silico clone cards for these plasmids. Before the start of the practical work, there is a knowledge check of the content taught via distance learning. In the practical course, students apply methods that have been theoretically developed in the lecture Methods of DNA Analysis and in the seminar Molecular Biology & Biophysical Methods. Type of protocol: Protocol in the form of a scientific publication - abstract, introduction, M&M, results, discussion, literature.

Activating methods

Continuous assessment: Preliminary work, inaugural examination, laboratory work, protocol

• Introduction to microbiological work (sterile work, disinfection), occupational health and safety regulations

• Isolation, cultivation and identification of microorganisms

• Cell counting

• Media preparation

• Microscopy and staining methods

• Morphological, biochemical and physiological characterization (differentiation methods)

Activating method

Continuous assessment: Cooperation and motivation, analysis report, poster, final presentation

The Molecular Biology and Biophysical Methods course covers 14 topics in molecular biology, from basic techniques such as nucleic acid purification and PCR to more advanced concepts such as protein expression and purification, protein-nucleic acid interactions, and sequencing. Students work in groups to research and present one of these topics. In the process, they develop both a presentation and a handout that serves as the basis for the final exam. The course covers topics such as gel electrophoresis, spectrophotometry, Southern blotting, different types of PCR, SDS-PAGE & Western blotting and the cultivation of microorganisms. It also examines antibodies and their applications, centrifugation techniques, Northern blotting, RT(q)-PCR, protein purification methods, various protein expression systems, protein-nucleic acid interactions, fluorescence in molecular biology, various sequencing methods, isolation and purification of nucleic acids from various organisms, and the use of primers and hybridization. The elaborated topics are disseminated to the students with the help of a jigsaw puzzle.

Presenting & activating methods, jigsaw puzzle

Final exam: Collaboration - jigsaw puzzle, written final exam

• Scientific writing and reporting:

• Develop the ability to write clear and concise scientific reports, including laboratory reports, journal articles and theses.

• Gain an understanding of the structure and essential components of scientific documents, such as abstract, introduction, methods, results, discussion, conclusions, and references.

• Presentation skills:

• Gain knowledge in preparing and delivering effective presentations on scientific topics.

• Learn to present both individually and collectively, use appropriate visual aids and engage the audience.

• Language skills:

• Improve English language skills in reading, writing, speaking and listening.

• Create and develop a personal language portfolio to track progress and set future language goals.

• CV and professional documentation:

• Acquire skills in writing a professional resume and cover letter.

• Understand the importance of presenting qualifications and experience effectively to potential employers.

• Ethical and transparent use of AI:

• Gain knowledge of ethical guidelines and legal frameworks for the use of Artificial Intelligence in academic work.

• Learn to transparently document and report on the use of AI tools in scientific research and communication.

• Critical thinking and self-reflection:

• Participate in self-reflection and peer feedback activities to assess and improve personal strengths and weaknesses in language and presentation skills.

• Develop strategies for continuous improvement and overcoming challenges in academic and professional settings.

• Critically evaluate the validity of references and sources in academic publications.

• Lecture with structured exercises

• Dialogue and discussion

• Individual work

• Group work

• Supervised distance learning

• Self-study

• Blended learning

• Guided self-reflection

• Peer feedback

• Problem-based learning

Continuous assessment: Immanent performance review

Performance and progress are assessed on an ongoing basis. The assessment is based on all written and oral work during the semester. Daily participation is also taken into account.

The course builds on the content of the "Social Skills (1st and 2nd semester)" module. The focus is on preparing students for cooperation in project teams and possible conflict situations in everyday working life. In the third semester, the focus is on team development and conflict resolution. Based on practical experience, team processes and factors influencing the productivity of teams are analyzed and ways of shaping them are developed. The causes of conflicts, typical behavioral patterns in conflict situations and their effects are reflected upon. Case studies and exercises are used to try out unconstructive and constructive conflict resolution. The main topics are team development and conflict resolution, working group or team, phases in team development, roles in the team, analysis of conflicts, phases of conflict escalation, strategies for dealing with conflicts

Lecture, individual and group work, practical implementation tasks, self-assessment through exercises for self-reflection and individual application, practical exercises with feedback and analysis

Continuous assessment: Immanent performance review, standard

National and international requirements and their implementation using a practical example in pharmaceutical companies in particular: Excerpts from

i. the Medicinal Products Act,

ii. the Medicinal Products Operating Regulations,

iii. Good Manufacturing Practice,

iv. Good Clinical Practice

v. Good Laboratory Practice,

vi. Good distribution practice

and the main features of qualification and validation with special consideration of quality risk management in accordance with the ICH Q9 guideline.

• Lecture

• Dialogue and discussion

• Individual work

• Group work

• Supervised distance learning

• Blended learning

• Problem-based learning

• Project work

• Reflection

Final exam: Assessment of a specific project work - development of an operating license - as well as a written final examination.

The content ranges from general terms and definitions of project management to project development, project planning, implementation and control through to project completion.

i. General terms and basics: definition of project and project management, differences between project/process, when does a task become a project, overview of project types, pros/cons of projects, organizational forms and project phase

ii. Project initialization: principles of idea development, from the idea to the project assignment (project charter), team formation and development, stakeholder analysis, governance

iii. Project planning: basics, task planning, process planning, scheduling, cost and resource planning, risk management

iv. Project implementation and control: basics of monitoring and control (deadlines, costs, performance, risk), project reporting,

v. Project completion: handover of results, final analysis, lessons learned, project team dissolution

• Lecture with structured exercises

• Dialogue and discussion

• Individual work

• Group work

• Blended learning

• Problem-based learning

Continuous assessment: Assessment of a specific project work - development of an operating license - as well as a written final examination.

In "Social Skills IV", the focus is on moderated problem solving. The planning and implementation of moderations in line with the assignment are practiced, various moderation methods are tried out and evaluated according to the task. Awareness of rhetorical tricks is sharpened and dealing with disruptions is practiced. The main topics are moderation and problem solving, moderation preparation, moderation methods, rhetorical strategies, dealing with disruptions, conducting discussions in an audit

• Lecture

• Individual and group work

• Practical implementation tasks

• Self-assessment through exercises for self-reflection and individual application

• Practical exercises with feedback and analysis

Continuous assessment: Performance and progress are assessed on an ongoing basis. The assessment is based on all written and oral work during the semester. Collaboration is also taken into account.

The course "Gene Regulation" examines the complexity of gene expression in prokaryotic and eukaryotic organisms. The course covers the following topics: Structure and function of bacterial genomes, ribosomal RNA operons, the mechanisms of RNA-dependent RNA polymerases, the regulation of HIV gene expression, and the revolutionary CRISPR-Cas9 system lies. It deals with how bacterial genomes are organized and compacted, what role nucleoid-associated proteins ??play in this process and how DNA supercoiling influences gene expression. The course then turns to ribosomal RNA operons and examines their organization, transcription and processing in prokaryotes and eukaryotes, emphasizing the importance of RNA polymerase I in this process. The course also deals with RNA-dependent RNA polymerases, enzymes that are crucial for the replication of RNA viruses such as coronaviruses and influenza viruses. Students will learn about the mechanisms that these viruses use to effectively replicate their genomes, such as ribosomal frameshifting and cap-snatching. The focus then shifts to HIV, where the complex transcriptional and post-transcriptional regulation of HIV-1 gene expression is covered. The functions of regulatory proteins such as Tat, Rev, Nef, Vif, Vpr and Vpu and their effects on viral replication are examined in more detail. Finally, the course will conclude with a detailed look at CRISPR systems, bacterial adaptive immune systems that have been repurposed for various biotechnological applications. Students will learn about the mechanism of CRISPR-Cas9, its role in gene editing, transcriptional regulation and epigenetic modification, and its potential for disease research.

Presenting method

Final exam: Written final exam

Based on the structure and properties of DNA, genes, chromatin and RNA in prokaryotes and eukaryotes, the regulation and expression of genetic information is discussed. The development and repair of DNA damage and the results of mutations are discussed. Epigenetic effects are discussed on the basis of the structure of chromatin. Signaling processes of the cell are presented using selected examples. Finally, applications of DNA technology in research and therapy are discussed.

Presenting method

Final exam: Written final exam on the computer (multiple choice)

This course provides hands-on laboratory experience focusing on the expression and purification of a recombinantly expressed protein. Students will gain knowledge in basic molecular biology techniques while exploring the expression and purification of this protein. The course takes a two-pronged approach:

? Small scale expression and detection: Students will induce expression using IPTG and track cell density over time, creating a growth curve. SDS-PAGE is then used to separate the expressed proteins. These separated proteins are visualized using Coomassie staining or further analyzed by Western blot using a specific antibody against the protein.

? Large-scale purification: The process includes cell lysis, centrifugation of the lysate and purification of proteins using Ni-NTA affinity chromatography. The purified protein is dialyzed against PBS to remove impurities and exchange the buffer. Finally, the Bradford test using a standard curve generated with bovine serum albumin (BSA) is used to determine the concentration of the purified protein.

At the end of this course, students will have the essential skills and knowledge to express and purify recombinant proteins using common molecular biology techniques. Furthermore, a comprehensive scientific protocol ("lab report") will be prepared by the students.

Activating method

Final exam: Protocol, written final exam, motivation, cooperation, practical skills, results

Energy and matter flow through the biosphere, thermodynamics of biochemical processes: Role of ATP, group transfer potential, coupling of reactions and Le Chatelier's principle, open systems, steady state, substrate chain and oxidative phosphorylation, biological redox reactions.

Basic catabolic (energy-yielding) & anabolic (biosynthetic) metabolic pathways: carbohydrate, fatty acid, cholesterol, nitrogen, amino acid, nucleotide metabolism, citrate cycle, regulated protein degradation (proteasome, autophagy). Includes biochemical reactions, enzymes and coenzymes/vitamins (including their mechanism using selected examples), energy balancing and the causes of some major metabolic diseases.

Regulation and integration of metabolism: concept of the pacemaker and "committed steps", avoidance of idle cycles, substrate channeling, iso(en)zymes, regulation of enzyme activity, examples of hormonal regulation of metabolic reactions and the associated signal transduction mechanisms.

Methods for the elucidation of metabolic pathways, metabolomics/metabonomics, metabolic flux, brief overview of metabolic control analysis (MCA).

Presentation of current examples of biotechnological and medical issues from the original literature.

• Lecture with structured exercises

• Dialogue and discussion

Final exam: Written final exam (multiple choice part, essay questions)

A) Spectroscopic methods: The principle of spectroscopic methods, ultraviolet-visible

spectroscopy, infrared spectroscopy, atomic absorption spectroscopy, flame photometry

(atomic emission spectroscopy), fluorescence spectroscopy, mass spectrometry,

X-ray structure analysis, nuclear magnetic resonance spectroscopy

B) Separation methods - 1. chromatographic methods: the principle of chromatographic methods,

Detailed discussion of chromatographic methods (categorized by separation principle), evaluation of chromatograms.

of chromatograms. 2. electrophoretic methods: General principles,

Detailed discussion of the electrophoretic methods

Lecture with active involvement of the students

Final exam: Written final exam

1. introduction to artificial intelligence (AI):

• What is AI? Basic terms such as "algorithm", "machine learning" and "artificial intelligence" easily explained.

• Practical examples: How AI is used in medicine and biotechnological research.

2. AI in biotechnology:

• Where and how AI is being applied in biotechnology. Where there are current developments.

• Examples: AI for analyzing DNA data or optimizing drug development.

• Get to know simple tools and platforms.

3. ethical and social issues:

• Discussions: Benefits and challenges of AI in biotechnology.

4. practical insights and teamwork:

• Group projects: Analyze and present case studies on AI applications in biotechnology.

Small programming projects on the application and interpretation of AI tools.

Performing & activating methods

Final exam: Working on examples and self-test with Moodle

In this course, students are taught the theory of basic protein chemistry techniques. A preparative purification of proteins is carried out, proteins are analytically detected, enzyme kinetic methods and the first steps of proteome analysis are carried out. The evaluation and interpretation of biochemical experimental data and the presentation of these scientific data are taught.

The following practical laboratory examples are carried out by the students:

Enzyme kinetics: photometry, Lambert-Beer's law, Michaelis-Menten kinetics, direct representation of data, Lineweaver-Birk diagram, influence of inhibitors on the kinetic constants Km and Vmax, inhibitor types, determination of IC50 values.

Protein chemical methods for preparative enzyme purification and for the first phase of proteome analysis: Preparation of buffers, cell disruption methods (mixer, douncer), cell fractionation, reversible and irreversible precipitation of proteins (ammonium sulphate, heat, acid), centrifugation, dialysis, ion exchange chromatography, direct and indirect enzyme assay, quantitative protein determination (Bradford), electrophoretic techniques (SDS-PAGE for purity control and molecular weight determination of proteins using Rf values; 2D electrophoresis; Coomassie Blue and silver staining).

Creation of a purification table.

Type of protocol: Three experiments, one protocol per experiment in the form of a scientific publication - abstract, introduction, M&M, results, discussion, literature.

Lecture, activating methods, group work, practical exercise

Final exam: 30% written examination on the theoretical background at the beginning of the internship,

40% assessment of oral and practical participation in the laboratory,

30% assessment of the protocol

• Risk assessment and safety management:

• Ability to conduct comprehensive risk assessments for laboratory work.

• Identification of hazardous substances, assessment of exposure potential and implementation of appropriate control measures.

• Understanding of EU chemical safety regulations (Dangerous Substances Directive, REACH, CLP).

• Scientific analysis and presentation:

• Analyzing complex scientific articles and summarizing key findings in concise presentations.

• Preparation and delivery of scientific presentations using electronic media.

• Focus on clarity, timing and audience engagement.

• Advanced English language skills:

• Improving the use of different English tenses through practical exercises and examples.

• Strengthen reading, writing, speaking and listening skills in scientific and technical contexts.

• Critical evaluation and peer feedback:

• Competence in critically evaluating academic work, including undergraduate theses, according to established criteria.

• Giving and receiving constructive feedback.

• Participation in collaborative work such as group discussions and peer review activities.

• Preparation for undergraduate thesis and professional development:

• Understanding the process and criteria for writing and evaluating an undergraduate thesis.

• Reflecting on internship experiences and integrating feedback into professional development plans.

• Lecture with structured exercises

• Dialogue and discussion

• Individual work

• Group work

• Supervised distance learning

• Self-study

• Blended learning

• Guided self-reflection

• Peer feedback

• Problem-based learning

Continuous assessment: Immanent performance review

Performance and progress are assessed on an ongoing basis. The assessment is based on all written and oral work during the semester. Daily participation is also taken into account.

1. General principles, methods and possible applications of stem cells and organoids
2. Brain organoids: production and comparison to the corresponding organ
3. Blood vessel organoids: production and comparison with the corresponding organ
4. Heart organoids: production and comparison with the corresponding organ
5. Kidney organoids: production and comparison to the corresponding organ
6. Intestinal organoids: production and comparison to the corresponding organ

New methods in organoid research (single cell RNA-sequencing, organoids-on-chip, screening approaches, vascularization

Lecture with discussion

Final exam: Written final exam

1. handling of routine cell cultures (splitting, cryopreservation, live/dead determination)

2. growth curve (evaluation of doubling time and influence of changed culture conditions)

3. cell cycle/mitosis stages

4. cytoskeleton/transfection

5. problem based task (theoretical)

Type of protocol: 4 experiments each with introduction, M&M, results and discussion, bibliography at the end.

Activating methods:
Lecture, work assignment via Moodle, practical group work with feedback, presentation of an example of problem-based learning

Continuous assessment: Reading comprehension test on Moodle

Ongoing assessment of practical work (technical skills and cooperation)

Final discussion (with examination character) and presentation of the problem-based assignment

Written individual report

In this undergraduate course, students are offered guidance and support in scientific theory, research practice and the formal aspects of research. Students are encouraged to explore scientific theories and methods and to select a research topic in the field of molecular biotechnology. The bachelor thesis itself is an extended work protocol based on the student's professional internship and requires him/her to document and scientifically reflect on his/her internship experience. The Bachelor's thesis covers the entire internship and is supervised by the internship supervisor. The Bachelor's thesis is not only an important part of the Molecular Biotechnology degree program, but can also be used as a mobility window for students who are interested in an internship abroad. The Bachelor's thesis is supervised by the internship supervisor. Students receive reflective feedback on their Bachelor's thesis.

Activating method

Final exam: Assessment by assessors

The professional internship offers students the opportunity to gain practical experience in a real biotechnological environment and thus bridge the gap between academic studies and professional practice. Students are responsible for finding both an internship position in a biotechnology company or research institute and a supervisor who is a specialist in the field. They gain observational experience in the daily operation of a biotechnology workplace and carry out independent scientific work. This allows students to apply their knowledge and skills to real research questions. The internship focuses on the development of key biotechnology skills, methodological approaches to research and problem solving, and important soft skills. Students document their experiences and findings in a comprehensive internship report (Bachelor's thesis). They also gain experience in documenting scientific results, which may include compliance with industry standards such as GMP ("Good Manufacturing Practice") and GLP ("Good Laboratory Practice") guidelines.

Activating methods

Continuous assessment: Expert opinion of the supervisor incl. grading

Fundamentals of private law: The characteristics of private law, its sub-matters and the relationship to public law are dealt with.

Corporate and company law: Basic concepts of corporate and company law are explained, as well as common features of the different forms of company. The most important forms of company in Austria (AG, GmbH, OG, KG, GesbR, Stille Gesellschaft, cooperatives) are presented from formation to termination, including questions on formation, executive bodies, rights and obligations of shareholders, internal and external relationships and termination.

Labor law: Covers the establishment and termination of employment relationships, differentiation from other types of contracts, non-competition, rights and obligations of employees and employers, and employee protection.

Patent law: Introduction to patent law and differentiation from other industrial property rights and copyright law. Topics include protection requirements, exclusion rights, national granting procedures, enforcement of rights, licensing options and international patent law.

• Lecture with interactive character

• Dialogue and discussion

Final exam: Written final exam

Based on the concept of business administration and operations, the economic advantages and disadvantages of the different legal forms of companies are discussed. We will deal with aspects of value creation and common key figures relating to company organization. This course focuses on strategic goals and management methods. Building on this, strategic and then operational marketing will be presented. Subsequently, fields of action in personnel policy will be presented. The course concludes with the requirements of external accounting.

• Lecture

• Dialogue and discussion

Final exam: Written final exam

The course presents core topics of everyday business life in biotech companies and deals with aspects that are both new and important for young employees in biotech R&D, operations and management in their everyday work (1.).

In particular, topics relating to the relationship between employees and superiors or company management are discussed and illustrated using case studies in break-out team sessions (2.).

Finally, soft skills and personal development are discussed from a practical perspective in context and illustrated using case studies in break-out team sessions (3.).

1. Everyday business life in biotech companies

1. Foundation & Founder

1. Funding & investors

1. Management & corporate bodies

1. Startups in the VUCA World - Managing Uncertainty

1. Dynamic Capabilities

1. Lean Startup concept

1. Innovation management

1. Agile & Teamwork - Example: Scrum

1. Company Culture

1. Employee - Leadership Relationship

1. Organizational Structures

1. Goal Setting

1. Performance Review

1. Feedback Culture

1. Soft Skills & Personal Development

1. Personal Development & Objective Agreement

1. Time Management & Efficiency

1. Communication

1. Entrepreneurial Mindset

1. Resilience

• Presenting method (lecture)

• Case study work in break-out team sessions

Continuous assessment: Immanent performance assessment (cooperation, homework, seminar presentations in group and individual work)

i. The components of the marketing mix and an integrated marketing strategy in relation to products, brands and companies

ii. Instruments of market research

iii. Market segmentation, market positioning, processing of target groups

iv. Methods of developing a price or profit model, basics of price calculation and adjustments

v. Regulatory mechanisms for pricing in Austria and on a global level

vi. Distribution and logistics

vii. Advertising, sales and communication in general, and specifically in a science-oriented environment

viii. The stages of product development with particular reference to pre- and post-launch pre-clinical and clinical studies for drugs

ix. Ethical principles of marketing

x. The product life cycle model

xi. Basics of portfolio analysis (portfolio matrix according to the Boston Consulting Group)

• Lecture with structured exercises

• Dialogue and discussion

• Individual work

• Group work

• Problem-based learning

Continuous assessment: Exercises and presentation during the ILV

- Case studies: Development of selected drugs (biopharmaceuticals and small molecules)

- Classes of pharmaceuticals

- Clinical (randomized controlled trials (RCTs)) and epidemiological study designs in the product life cycle

- Endpoints and inclusion and exclusion criteria

- Special patient groups

- Data analysis and interpretation

- Overview: Ethical aspects, origins and principles of Good Clinical Practice (GCP)

- International guidelines (EMEA, FDA, ICH)

- Product life cycle management and selected commercial aspects

- Interfaces: Marketing, in particular the marketing mix ("4 Ps") and the product life cycle

• Lecture with structured exercises

• Group discussions

• Problem-based learning

Final exam: Final examination: Written final examination, assessment of exercises during the ILV

1) Microscopy, preparation technique: basics of microscopic technique, cross-section of classical light microscopic methods, foray through current high-resolution light and electron microscopy, cryo techniques. Histological preparation techniques from fixation and sectioning to immunolabeling.
-tissue science
-connective/supportive tissue
-muscle tissue
-nerve tissue:

2) Organology: Introductory basic building principle of the organ / organ system with emphasis on structure " functional relationships.
-circulation
-digestion
-excretion
-reproduction
-skin
-endocrine system
-respiratory tract
-lymphatic organs
-stem cells
-barriers in the organism

Presenting & activating methods:

• Lecture with permanent feedbacksupplemented by online - virtual microscopy

• short films

• formative mentimeter test.

Final exam: Combined written exam: multiple choice questions, open questions and topic elaboration including sketches

Homeostasis and membrane potential (compartments, transport mechanisms, resting membrane potential, action potential, conduction); heart (structure of the heart, conduction system, pacemaker, ECG, course of a normal cardiac action, coronary perfusion); respiration (lung volumes, respiratory cycle, respiratory restriction, compliance, surfactant, O2 resp. CO2 transport; musculature (electromechanical coupling, contraction, striated, smooth and cardiac muscles, performance diagram); circulation (body & pulmonary circulation, fetal circulation, pressure ratios, oxygen saturation, oxygen demand of important organs, local blood flow regulation); Blood (transport of nutrients and waste products, storage, coagulation, plasma proteins); Defense (cellular & humoral mechanisms, AB0 blood group system, complement system, course of inflammation); Kidney (structure of a nephron, glomerular filtration, secretion, reabsorption, regulation of blood volume & electrolyte composition, renin-angiotensin-aldosterone system); Metabolism/digestion (sections of the gastrointestinal tract and their functions, digestion/absorption of carbohydrates, proteins and fats, functions of the liver); sensory organs (general sensory physiology, sense of touch, depth sensitivity, photoreceptors, organ of balance, ear, sense of smell, sense of taste, perception of pain); Nervous system (autonomic nervous system, transmitter systems, motor functions, cognitive functions); endocrinology (most important hormone receptor mechanisms, hormones of the pituitary gland, regulation of blood sugar levels, catecholamines, glucocorticoids, thyroid hormone, sex hormones).

• Lecture

• Dialogue and discussion

Final exam: Written final exam

Presentation of biological models in medicine and basic research, starting with unicellular organisms, as well as fish, frog, chicken, mouse models, Drosophila and C. elegans as invertebrate models). Criteria for the use of model organisms, with a focus on genetic methods. Genome research in model organisms, disease models in biomedical research, targeted production of animal models using genetic manipulations such as CRISPR/Cas9.

Implementation and legal basis of animal experiments in research and in the approval of medicinal products.

• Lecture

• Dialogue and discussion

Final exam: Written final exam on the computer (multiple choice)

Natural regenerative capacity of tissues (human-animal comparison) and influencing these capacities, application of implants and organ transplants (problem of immune reactions), bone marrow transplantation Introduction to biomaterials - in particular to the class of biodegradable materials, properties and function of stem cells (differentiation potential), Extracellular carrier materials for three-dimensional implants (matrix-cell interaction), cell therapy by encapsulation of cells, special process techniques for tissue culture in tissue engineering, use of growth factors in regenerative medicine, problem of immune reactions when administering therapeutic proteins, production of artificial tissue, status quo of tissue engineering in various tissues. In particular, tissue engineering of skin, cartilage or bone tissue, use or production of autologous and artificial vascular prostheses, regeneration of heart muscle tissue, regeneration of nerve tissue for the treatment of injury to the peripheral and central nervous system and degenerative diseases of the central nervous system. Ethical principles of organ transplantation, the use of stem cells and the use of artificial tissue produced by tissue engineering. Students are given an overview of the preclinical and clinical development of artificial tissue using tissue engineering. The complexity of both the production and registration of such drugs is highlighted. Subsequently, students also gain an insight into the commercial situation of products manufactured using tissue engineering.

Presenting methods:

• Lecture with PowerPoint presentation

Activating methods:

• View specimens of biomaterials

• Videos for the visualization of production techniques of artificial tissues or organs by means of tissue engineering

Final exam: Written final exam

Developmental biology

1. Basic principles of development

• Mechanisms of differentiation, growth and pattern formation.

• Role of induction, morphogens and cytoplasmic determinants in regulatory development and cell fate determination.

1. Stem cells and regeneration

• Concepts of stem cells, differentiation and determination.

• Mechanisms of regeneration and their biological potential.

1. Phases of embryonic development

• Processes of early cell division, gastrulation, neurulation and organ development.

1. Axis formation

• Formation and control of the anteroposterior, dorsoventral and left-right axes, including the role of organizers and Hox genes.

1. Model systems in developmental biology

• Analysis of development in Drosophila melanogaster, C. elegans, zebrafish, Xenopus, chickens and mice and an evolutionary comparison of the mechanisms.

1. Methods of developmental biology

• Experimental approaches such as transplantation, gene expression analysis, gain-of-function and loss-of-function methods.

1. Regulation of growth

• Mechanisms of growth control in embryonic and post-embryonic development.

Carcinogenesis

1. Basics of tumor development

• Monoclonal origin of tumors and the selection of tumor cells.

• Slow, multistage development of cancer with the role of mutations and DNA repair mechanisms.

1. Mutagens and tumorigenesis

• Effects of mutagens and promoters such as inflammatory processes.

• Influence of environmental factors, e.g. radiation, carcinogenic substances and nutrition.

1. Mechanisms of tumor progression

• Processes of metastasis and the interaction of tumors with the immune system.

• Viral risk factors and their role in the development of cancer.

1. Molecular basis of cancer

• Oncogenes, tumor suppressor genes and their role in the "Hallmarks of Cancer".

• Significance of apoptosis, senescence, telomerase, angiogenesis and epigenetic changes.

1. Modern cancer therapy

• Analysis of central signaling pathways in the development of cancer and their significance for innovative therapeutic approaches.

• Lecture

• Dialogue and discussion

Final exam: Written final exam on the computer (multiple choice)

The aim of this course is to explain step by step the path from the biological or pathological pathway to the identification of the genes involved (using the methodology of functional genome research) and then the targeted search for specific active substances through to clinical studies. The first step is an introduction to the medically relevant signalingpathways of the cell and the basics of immunology. The methods of genome research are then presented, starting with bioinformatics and the use of existing databases. Statistical methods, which are used for all activities 'From bench toBedside' are explained and discussed in detail.High-throughput methods based on microarrays and proteomics make it possible, candidate genes identify candidate genes that fulfill functions in the desired biological/pathological pathways pathways. Narrowing down these potential targets takes place during the functional characterization of the candidate genesstarting in cell culture systems and finally in the context of the whole organism. The next step is to find low-molecular substances that modulate the function of the biologically validated target. For this purpose, in vitro and in vivo test systems must be established in order to create substance libraries (up to 2 million compounds). Biophysically, structurally and biochemically validated "hits" are optimized for potency, bioavailability, specificity and toxicity. In an iterative process, the newly synthesized derivatives are tested for their optimized properties in the systems established in vitro and in vivo in order to ultimately identify a lead structure. This will be tested in preclinical models for therapeutic efficacy and potential side effects analyzed in preclinical models. Once the requirements profile of the lead compound has been met, the clinical trial phase can begin.

• Lecture

• Dialogue and discussion

Final exam: Written final exam

The focus is to outline to students the most important steps on the exciting path from idea to product development to marketing:

1. Idea to market

• What is innovation?

• The path from idea to research, development (R&D) and approval.

• Markets, diseases & therapeutic areas (indications)

• TEAM CASE 1: Outline of an innovation process using an example

1. How is a pharmaceutical company organized?

• TEAM CASE 2: Outline of an example organization in teamwork

1. Important players & organizational forms in the biopharma sector.

• Typical organizational forms

• Examples

1. What are the main classes of pharmaceuticals?

• Small molecules ("small molecules")

• Biologics

1. What are biomarkers and their importance in drug development?

• Classification of biomarkers

• Important application examples of biomarkers

1. What is personalized precision medicine?

• Explanation of the terms personalization & precision medicine

• Application example cancer therapy

1. Pharma R&D

• The role of molecular biology

• Target discovery - molecular patho-mechanisms

• Screening methods (HTS, high content imaging ...)

• Bioinformatics, Data Science & AI

• Hit to Lead (H2L) optimization

1. Drug pipeline, preclinical & clinical development

• In vitro & in vivo models

• Tocicology and ADME

• Phase 1- 3

• GLP & GCP

1. Brief overview of regulatory affairs & drug approval

• Regulatory Affairs (FDA, EMA, etc.) & Approval

• Production & GMP

1. Conclusion Team Case

TEAM CASE 3: Refinement of the sketch of an example organization in team work

• Lectures

• Interactive discussion

Continuous assessment: Homework, seminar presentations in group and individual work

1. Introduction to laboratory automation (lecture)

• Overview of systems and areas of application in biotechnology

• Advantages and challenges of automation

• Components of automated systems: pipetting robots, liquid handling systems, sensor technology

1. Fundamentals of robotics (lecture)

• Mechanics and programming of laboratory robots

• Interfaces and data integration (LIMS)

• Fundamentals of motion planning and automation software

1. Automation forms & concepts (lecture)

• Automation concepts & methods

• Automation equipment

1. Regulation, validation & qualification

• Regulatory aspects of automation

• Equipment validation & validation planning (DQ, IQ, OQ, PQ)

• What is an audit trail?

• SOPs & employee qualification

1. Application examples and practical relevance (lecture)

• Automated sample preparation and assays (e.g. qPCR, ELISA)

• Screening and high-throughput analyses in research and industry (HTS)

• Quality assurance and validation of automated processes

1. Practical case with an Opentrons OT-2 in teamwork (internship)

• Planning and protocol design for a 2-dimensional dilution series

• Programming of the robot (Visual Point & Click vs. Python API-based)

• Implementation of the protocol incl. troubleshooting

• Analysis and interpretation of data from the automated process

1. Lab - report from the practical case (seminar)

• Presentation & discussion of the team results

1. Future of laboratory automation (lecture & discussion)

• Trends in robotics and AI for laboratory applications in research & industry

• Ethics and labor market changes through automation

Lecture (70%), practical course (15%), seminar (15%)

• Lectures

• Group exercise

• Presenting methods

• Activating methods Lecture

Final exam: Assessment of participation and performance in the group exercise with presentation during the course. Written examination at the end of the course. The theoretical examination includes multiple-choice and open questions.

The Bachelor's examination is the final milestone of the Bachelor's degree program in Molecular Biotechnology. The Bachelor's examination takes place before a relevant examination board. This comprises a presentation in which the student presents the results of his/her professional internship, i.e. the Bachelor's thesis, a questioning of the presentation and an oral examination in which the students demonstrate the knowledge and skills they have acquired. The examination covers key topics in molecular biotechnology, including molecular biology, cell biology, biochemistry, biotechnology and their methodological knowledge. The aim of the examination is to prepare students for their future professional challenges and to confirm their suitability for further studies or professional activities in the field of biotechnology.

Activating methods: presentation and oral examination

Final exam: Up to 20 points are awarded by the examination senate for the presentation.

Up to 20 points are also awarded for the subsequent questioning of the presentation.

Up to 30 points are awarded for answering the questions on central theoretical and practical topics of the Bachelor's degree program.

The sum of these points results in the overall grade for the Bachelor's examination

Part 1: Self-reflection:

• Guided self-reflection on various aspects of the work placement, including working environment, tasks undertaken, skills acquired and personal insights.

• Topics include the assessment of prior knowledge, the importance of specific competencies and the evaluation of laboratory techniques used during the internship.

Part 2: Group Reflection:

• In groups, reflect, discuss and present self-selected topics related to their professional internship experiences - possible topics include preparation for international internships, challenges during the internship, the application process, personal development and comparison between academic and industry environments.

• Each group will create a presentation in a chosen format (e.g. poster, website, film, podcast) to sharetheir collective insights with their fellow studentsand the students to follow .

• Lecture

• Dialog and discussion

• Individual work

• Group work

• Supervised distance learning

• Blended learning

• Project work

• Research-based learning

Continuous assessment: Active participation.

This course is indirectly linked to the BP Reflection course. I.e. in this course, which should take place before the course Biotech Careers, the students reflect on their experiences with regard to methodological skills but also their experiences/opinions/conclusions etc. during the internship. Based on the learning outcomes of this course, in the first part of this course : Biotech Careers, all current options for different career paths in industry and academia will be presented and reflected in discussion with the group.

The second part will be organized together with the BTA (alumni association), which offers students the opportunity to get to know people from different career fields in industry and academia and to ask questions about these career profiles.

Activating method

Continuous assessment: Active participation