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β-Hairpin Folding Mechanism of a Nine-Residue Peptide Revealed from Molecular Dynamics Simulations in Explicit Water
The β-hairpin fold mechanism of a nine-residue peptide, which is modified from the β-hairpin of α-amylase inhibitor tendamistat (residues 15–23), is studied through direct folding simulations in explicit water at native folding conditions. Three 300-nanosecond self-guided molecular dynamics (SGMD) s...
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| Autori principali: | , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Biophysical Society
2004
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1304050/ https://ncbi.nlm.nih.gov/pubmed/15041639 |
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