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A statistical mechanical model for beta-hairpin kinetics.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Munoz, Victor Henry, Eric R. Hofrichter, Jürgen Eaton, William A. |
| Copyright Year | 1998 |
| Abstract | Understanding the mechanism of protein secondary structure formation is an essential part of the protein-folding puzzle. Here, we describe a simple statistical mechanical model for the formation of a beta-hairpin, the minimal structural element of the antiparallel beta-pleated sheet. The model accurately describes the thermodynamic and kinetic behavior of a 16-residue, beta-hairpin-forming peptide, successfully explaining its two-state behavior and apparent negative activation energy for folding. The model classifies structures according to their backbone conformation, defined by 15 pairs of dihedral angles, and is further simplified by considering only the 120 structures with contiguous stretches of native pairs of backbone dihedral angles. This single sequence approximation is tested by comparison with a more complete model that includes the 2(15) possible conformations and 15 x 2(15) possible kinetic transitions. Finally, we use the model to predict the equilibrium unfolding curves and kinetics for several variants of the beta-hairpin peptide. |
| File Format | PDF HTM / HTML |
| PubMed reference number | 9600886 |
| Journal | Medline |
| Volume Number | 95 |
| Issue Number | 11 |
| Alternate Webpage(s) | http://www.pnas.org/content/95/11/5872.full.pdf |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
