Packing helices in proteins by global optimization of a potential energy function.

ABSTRACT: An efficient method has been developed for packing alpha-helices in proteins. It treats alpha-helices as rigid bodies and uses a simplified Lennard-Jones potential with Miyazawa-Jernigan contact-energy parameters to describe the interactions between the alpha-helical elements in this coarse-grained system. Global conformational searches to generate packing arrangements rapidly are carried out with a Monte Carlo-with-minimization type of approach. The results for 42 proteins show that the approach reproduces native-like folds of alpha-helical proteins as low-energy local minima of this highly simplified potential function.

SUBMITTER: Nanias M 

PROVIDER: S-EPMC149897 | biostudies-literature | 2003 Feb

REPOSITORIES: biostudies-literature