BIOL 364 Lecture Notes - Lecture 1: Hsp70, Atp Hydrolysis, Alpha Helix
27 Sep 2016
School
Department
Course
Professor
Document Summary
Biol 364 molecular chaperones in protein folding and proteostasis. Proteins need to be in their native state to function. Proteostasis is achieved via molecular chaperones and their regulators, which assist in de novo folding or refolding, and the ubiquitin-proteasome system (ups) and autophagy system, which mediate the timely removal of irreversibly misfolded and aggregated proteins. The amino acid sequence, encoded in the dna, contains all of the necessary information to specify the three-dimensional structure of a protein. The folding of small proteins becomes considerably more challenging in vivo, because the cellular environment is highly crowded: increases the tendency of non-native and structurally flexible proteins to aggregate. Some basics on protein folding and how it can go awry. Folding reactions are highly complex and heterogenous, relying on the cooperation of many weak, non- covalent interactions. Hydrophobic forces are particularly important in driving chain collapse and the burial of non-polar amino-acid residues within the interior of the protein.
