A simple model for calculating the kinetics of protein folding from three-dimensional structures.

ABSTRACT: An elementary statistical mechanical model was used to calculate the folding rates for 22 proteins from their known three-dimensional structures. In this model, residues come into contact only after all of the intervening chain is in the native conformation. An additional simplifying assumption is that native structure grows from localized regions that then fuse to form the complete native molecule. The free energy function for this model contains just two contributions-conformational entropy of the backbone and the energy of the inter-residue contacts. The matrix of inter-residue interactions is obtained from the atomic coordinates of the three-dimensional structure. For the 18 proteins that exhibit two-state equilibrium and kinetic behavior, profiles of the free energy versus the number

SUBMITTER: Munoz V 

PROVIDER: S-EPMC18030 | biostudies-literature | 1999 Sep

REPOSITORIES: biostudies-literature