Subsections
[Cr:4, Lc:3, Tt:0, Lb:0]
- The protein folding problem and the Levinthal paradox.
- The conformational description of polypeptide chains in good and poor
solvents.
- The protein folding funnel and the energy landscape.
- Biophysical techniques in protein folding studies: CD, fluorescence,
NMR, H/D exchange, Time-resolved spectroscopy, Laser T-jump and fast
mixing.
- Unfolding and folding under equilibrium and kinetic conditions.
- Detection and characterizations of folding intermediates Case studies
on two-state, multi-state and downhill folding.
- Intrinsically disordered proteins and new paradigm in protein folding.
- Single-molecule studies in protein folding.
- Molecular chaperones and protein folding in the context of cells.
- Protein misfolding and aggregation leading to amyloid formation.
- Protein misfolding diseases: Alzheimer's, Parkinson's, Huntington's
and prion diseases.
- Prion biology: Self-replicating misfolded protein conformers and
non-Mendelian genetics.
- V. Muñoz, Protein Folding, Misfolding and Aggregation: Classical
Themes and Novel Approaches, 1st Edn., Springer (2008).
- A. R. Fersht, Structure and Mechanism in Protein Science: A
Guide to Enzyme Catalysis and Protein Folding, 1st Edn., W. H.
Freeman (1998).
- B. Nolting, Protein Folding Kinetics: Biophysical Methods, 2nd
Edn., Springer (2005).
