All-atom ab initio folding of a diverse set of proteins
| dc.creator | Yang, Jae Shick | |
| dc.creator | Chen, William W. | |
| dc.creator | Skolnick, Jeffrey | |
| dc.creator | Shakhnovich, Eugene I. | |
| dc.date | 2006-11-27 | |
| dc.date.accessioned | 2026-07-07T07:34:02Z | |
| dc.date.available | 2026-07-07T07:34:02Z | |
| dc.description | Natural proteins fold to a unique, thermodynamically dominant state. Modeling of the folding process and prediction of the native fold of proteins are two major unsolved problems in biophysics. Here, we show successful all-atom ab initio folding of a representative diverse set of proteins, using a minimalist transferable energy model that consists of two-body atom-atom interactions, hydrogen-bonding, and a local sequence energy term that models sequence-specific chain stiffness. Starting from a random coil, the native-like structure was observed during replica exchange Monte Carlo (REMC) simulation for most proteins regardless of their structural classes; the lowest energy structure was close to native- in the range of 2-6 A root-mean-square deviation (RMSD). Our results demonstrate that the successful all-atom folding of a protein chain to its native state is governed by only a few crucial energetic terms. | |
| dc.description | Structure, in press | |
| dc.identifier | https://arxiv.org/abs/q-bio/0611086 | |
| dc.identifier | http://arxiv.org/abs/q-bio/0611086 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/119667 | |
| dc.subject | Biomolecules | |
| dc.title | All-atom ab initio folding of a diverse set of proteins | |
| dc.type | text |