COURSES

Goals

Objectives: To enable students to understand the principles of protein folding and stability. Thermodynamic, kinetic and structural aspects are discussed. In addition, they become familiar with the associated mechanisms of protein aggregation which is involved in neurodegenerative diseases. Competences: get to know interdisciplinary fields of structural biology, biochemistry and biophysics. Independent and creative thinking; be able to formulate problems and open questions.

Curriculum

- Stability of proteins: basic knowledge of stability and its determination, - The problem of protein folding - folding in vitro and in vivo, - Kinetics, transition states and energy landscapes, - How does folding start? - detecting the early stages, - The molten globule - its relevance in folding, aggregation and protein translocation, - The enzymology of protein folding, - The role of chaperones in folding in vivo, - Aggregation to amyloid-fibrils: in vitro and in the cell, - Reversible condenstion of proteins into membrane-less bodies; similarity to gel-liquid phase separation - Protein folding and disease; neurodegenerative diseases.