Lecture 7: Protein Folding Flashcards
Amino acids that prefer alpha helix
M Methionine A Alanine L Leucine E Glutamate K Lysine R Arginine H Histidine Q Glutamine
Amino acids that prefer Beta sheet
C Cystein F Phenylalanine W Tryptophan T Threonine I Isoleucine Y Tyrosine V Valine
Amino acids that prefer reverse turn
S Serine N Asparagine D Aspartic acid G Glycine P Proline
Protein disulfide isomerase function
Properly positions sulfide bonds by re-arranging non-native S-S
S-S bonds in intra vs extracellular proteins
Intracellular lack S-S bonds
Extracellular typically have a few S-S bonds
HSP 70
ATP driven
Reverses misfolds; newly synthesized proteins; unfold/refold of trafficked proteins
HSP 90
For signal transduction proteins
Acts at late stage of folding of proteins
Chemicals that will denature
Detergents (SDS) Chaotropic agents (Urea) Organic solvents (TCA)
Circular dichromism
Used to study conformation of proteins in solution
Molecular chaperons
Bind to unfolded/partially folded polypeptide chains
Prevent improper association of hydrophobic segments
Non-native folding/aggregation will not occur
Allow misfolded proteins to refold into native conformation
Chaperonin mechanism
Unfolded polypeptide enters cylinder
Cylinder is capped and creates hydrophillic environment for protein to fold
Protein is released
Proteasome
Digests ubiqutinated proteins
26S proteasome consists of
2- 19S regulatory units
1- 20S catalytic core
19S
Recognizes ubiquitinated proteins
Isopeptidase cleaves ubiquitin
Directs protein into catalytic core 20S
20S
Catalytic core composed of 28 subunits
Sealed barrel, access controlled by 19S