Molecular dynamics simulations of -hairpin folding have been carried out with a solvent-referenced potential at 274 K. The model peptide V 4 D PGV 4 formed stable -hairpin conformations and the -hairpin ratio calculated by the DSSP algorithm was about 56% in the 50-ns simulation. Folding into -h
✦ LIBER ✦
Folding dynamics and mechanism of β-hairpin formation
✍ Scribed by Muñoz, Victor; Eaton, William A.; Thompson, Peggy A.; Hofrichter, James
- Book ID
- 109786892
- Publisher
- Nature Publishing Group
- Year
- 1997
- Tongue
- English
- Weight
- 376 KB
- Volume
- 390
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/36626
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Folding of beta-hairpin structures of synthetic peptides has been simulated using the molecular dynamics method with a solvent-referenced potential. Two similar sequences, Ac-MQIFVKS(D)PGKTITLKV-NH(2) and Ac-MQIFVKS(L)PGKTITLKV-NH(2), derived from the N-terminal beta-hairpin of ubiquitin, were used