Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures.

ABSTRACT: Guided by recent experimental results suggesting that protein-folding rates and mechanisms are determined largely by native-state topology, we develop a simple model for protein folding free-energy landscapes based on native-state structures. The configurations considered by the model contain one or two contiguous stretches of residues ordered as in the native structure with all other residues completely disordered; the free energy of each configuration is the difference between the entropic cost of ordering the residues, which depends on the total number of residues ordered and the length of the loop between the two ordered segments, and the favorable attractive interactions, which are taken to be proportional to the total surface area buried by the ordered residues in the native structur

SUBMITTER: Alm E 

PROVIDER: S-EPMC18029 | biostudies-literature | 1999 Sep

REPOSITORIES: biostudies-literature