772401 Basic course I - analysis, design and engineering of proteins

Type
Lecture
Semester hours
2
Lecturer (assistant)
Hofbauer, Stefan , Haltrich, Dietmar , Ludwig, Roland , Peterbauer, Clemens Karl , Schäffer, Christina , Traxlmayr, Michael , Schaffner, Irene , Obinger, Christian
Organisation
Offered in
Wintersemester 2024/25
Languages of instruction
Englisch
Content

1a: Chemistry of non-covalent interactions and structural building blocks in proteins (Haltrich)
1b: Protein diversity – evolution of structure and function (Haltrich)
1c: Protein structure I: X-ray crystallography (Djinovic-Carugo)
1d: Protein structure II: Cryo-EM (Heuser)
1e: Protein structure III: Electronic circular dichroism, fluorescence and Fourier transform infrared spectroscopy of proteins (Obinger)
1f: Protein structure IV: Self-assembling proteins - Light scattering, electron microscopy, atomic force microscopy (Schäffer)
1g: Measurement of protein – ligand (protein) interaction: isothermal titration calorimetry and surface plasmon resonance (Schaffner)
1h: Core facility Biomolecular & Cellular Analysis – practical considerations (Schaffner)
1i: Folding pathways, conformational and thermal stability of proteins (Obinger)
1j: Measurement of changes in stability – differential scanning calorimetry and more (Obinger)
1k: Enzyme kinetics: steady–state versus presteady–state kinetics (Ludwig)
1l: Mutagenesis: Site–directed mutagenesis, directed evolution by non–recombinative and recombinative methods (Peterbauer)
1m: Protein libraries: design and construction (Rüker)
1n: Surface display technologies (Rüker)
1o: Screening criteria and methods (Peterbauer)
1p: Case study: Engineered therapeutic antibodies (Rüker)
Previous knowledge expected

Study in biotechnology, food sciences and technology, (bio)chemistry, molecular biology, medicine or bioinformatics.
Objective (expected results of study and acquired competences)

Improved knowledge of structural biology of proteins, conformational and thermal stability, as well as (un-)folding pathway(s). Profound understanding of methods in analysis of protein structure, quality and stability.
Understanding of design of protein libraries, methods in mutagenesis, surface display technologies and screening strategies. Knowledge of methods for protein engineering and studies in enzyme kinetics and protein – ligand (protein) interaction.
You can find more details like the schedule or information about exams on the course-page in BOKUonline.