An alternative approach to protein folding.

ABSTRACT: A diffusion theory-based, all-physical ab initio protein folding simulation is described and applied. The model is based upon the drift and diffusion of protein substructures relative to one another in the multiple energy fields present. Without templates or statistical inputs, the simulations were run at physiologic and ambient temperatures (including pH). Around 100 protein secondary structures were surveyed, and twenty tertiary structures were determined. Greater than 70% of the secondary core structures with over 80% alpha helices were correctly identified on protein ranging from 30 to 200 amino-acid sequence. The drift-diffusion model predicted tertiary structures with RMSD values in the 3-5 Angstroms range for proteins ranging 30 to 150 amino acids. These predictions are among the be

SUBMITTER: Kang Y 

PROVIDER: S-EPMC3775432 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature