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
β-hairpin stability and folding: molecular dynamics studies of the first β-hairpin of tendamistat
✍ Scribed by Alexandre M.J.J. Bonvin; Wilfred F. van Gunsteren
- Book ID
- 115629954
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 633 KB
- Volume
- 296
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract The structural properties of a 10‐residue and a 15‐residue peptide in aqueous solution were investigated by molecular dynamics simulation. The two designed peptides, SYINSDGTWT and SESYINSDGTWTVTE, had been studied previously by NMR at 278 K and the resulting model structures were class
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