Chapter 4 Flashcards
peptide bonds in proteins
trans
rotation in peptide chain
two covalent bonds of Ca-C (psi) and N-Ca(phi)
globular shapes
polypeptide chain must frequently reverse direction
globular proteins
compact, spherical, and conduct most enzymatic activity
fibrous proteins
extended, insoluble, and usually fill structural roles in the cell
intrinsically disordered protein
lack defined secondary and tertiary structure until bound
quaternary structure
assembly of individual polypeptides into a larger functional cluster
denaturation
loss of structural integrity with accompanying loss of activity
proteins can be denatured by
-heat or cold
-pH extremes
-organic solvents
-chaotropic agents
anfinsen ribonuclease refolding experiment
-urea in the presence of 2-mercaptoethanol fully denatures ribonuclease
- when they are removed, protein refolds and current disulfide bonds are reformed
- protein sequence alone determines the native conformation
chaperones
do not actively promote the folding of the substrate protein but prevent aggregation of unfolded peptides