Protein structure prediction by all-atom free-energy refinement.

ABSTRACT:

Background

The reliable prediction of protein tertiary structure from the amino acid sequence remains challenging even for small proteins. We have developed an all-atom free-energy protein forcefield (PFF01) that we could use to fold several small proteins from completely extended conformations. Because the computational cost of de-novo folding studies rises steeply with system size, this approach is unsuitable for structure prediction purposes. We therefore investigate here a low-cost free-energy relaxation protocol for protein structure prediction that combines heuristic methods for model generation with all-atom free-energy relaxation in PFF01.

Results

We use PFF01 to rank and cluster the conformations for 32 proteins generated by ROSETTA. For 22/10 high-quality/low quali

SUBMITTER: Verma A 

PROVIDER: S-EPMC1832197 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature