Name
Abstract | ||
|---|---|---|
We have investigated the folding pathway of the 36-residue villin headpiece subdomain (HP-36) by action-derived molecular dynamics simulations. The folding is initiated by hydrophobic collapse, after which the concurrent formation of full tertiary structure and alpha-helical secondary structure is observed. The collapse is observed to be associated with a Couple of specific native contacts contrary to the conventional nonspecific hydrophobic collapse model. Stable secondary structure formation after the collapse suggests that the folding of HP-36 follows neither the framework model nor the diffusion-collision model. The C-terminal helix forms first, followed by the N-terminal helix positioned in its native orientation. The short middle helix is shown to form last. Signs for multiple folding pathways are also observed. (c) 2009 Wiley Periodicals, Inc. J Comput Chem 31: 57-65, 2010 |
Year | DOI | Venue |
|---|---|---|
2010 | 10.1002/jcc.21288 | JOURNAL OF COMPUTATIONAL CHEMISTRY |
Keywords | Field | DocType |
protein folding,molecular dynamics,pathway | Hydrophobic collapse,Protein folding,Crystallography,Protein tertiary structure,Computational chemistry,Chemistry,Downhill folding,Helix,Molecular dynamics,Villin,Protein secondary structure | Journal |
Volume | Issue | ISSN |
31.0 | 1 | 0192-8651 |
Citations | PageRank | References |
0 | 0.34 | 3 |
Authors | ||
3 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| In-ho Lee | 1 | 324 | 35.54 |
| Seungyeon Kim | 2 | 87 | 14.53 |
| Jooyoung Lee | 3 | 99 | 10.25 |