GENE 500 Lecture Notes - Lecture 4: Energy Landscape, Protein Folding, Ribonuclease
Document Summary
Although a small protein like ribonuclease can fold spontaneously, even it is slow by biological standards. In the cell, protein folding is assisted by chaperones and chaperonins. Chaperones help move proteins to and between energy states. Energy landscape limited by co-translation medium, hydrophobic residues form the internal core. Solvent is part of the process; in aqueous. Step 1: when bound to atp, the monomeric. Chaperonin-mediated protein folding help proteins fold at the expense of atp: using these mechanisms (chaperones and chaperonins), it leads to a much faster folding (kinetically) than folding without any help. Groel is a barrel-shaped complex of fourteen identical 60,000-mw subunits, arranged in two stacked rings (blue) of seven subunits each that form two distinct internal polypeptide folding chambers. Homoheptameric lids (10,000-mw subunits), groes (red), can bind to either end of the barrel and seal the chamber on that side. Step 1: a partly folded or misfolded polypeptide enters one of the folding chambers.
