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Studiendelegierter
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Foreign Applicants
Prof. Rudolf Glockshuber
Part I: Biophysics of protein folding and stability, R. Glockshuber (4 x 3 hours): General principles of protein folding and protein stability; Thermodynamics of protein folding; Protein folding kinetics and transition state characterization; Slow reactions in protein folding: X-Pro isomerization and SS bond formation; Spectroscopic techniques to study protein folding; Prions and amyloids
Part II: Enzymes and molecular chaperones, E. Weber-Ban (2 x 3 hours): Molecular Chaperones, definition and roles of molecular chaperones, specific examples of chaperones: Hsp70/40 chaperone system, GroEL/ES Chaperonin, Hsp100 / Clp proteins, Pilus chaperones. Enzymology: chemical catalysis and enzyme catalysis, theories on enzyme catalysis, enzyme kinetics, acceleration factors
Part III: RNA, F. Allain (1 x 3 hours): Catalytic RNA: Mechanisms and structure, Apatamers and SELEX, RNAi
Part IV: Structure and function of membrane proteins, K. Locher and F. Winkler (5 x 3 hours): Crystallization of membrane proteins, X-ray crystallography (practical considerations for assessing structural information and its quality), Functional assays of membrane proteins (in vitro reconstitution, cellular assays), Structural information from site-directed-spin-labeling (SDSL) and EPR (electron paramagnetic resonance) spectroscopy, Improved hydrophobicity scales of amino acids (partitioning into lipid bilayers). Biological themes (emphasis on structure function relationships, structural principles), Membrane Transporters, Ion channels, water channels (aquaporins), ammonia channels, Receptor tyrosine kinases (RTKs), specific examples
Part V: Protein analytics and proteomics, R. Brunisholz (1 x 3 hours): Edman Sequencing, MALDI-TOF mass spectrometry, Electrospray mass spectrometry, High throughput protein identification
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