Interplay between hydrophobic cluster and loop propensity in beta-hairpin formation: a mechanistic study.

ABSTRACT: We investigated the structural determinants of the stability of a designed beta-hairpin containing a natural hydrophobic cluster from the protein GB1 and a D-Pro-Gly turn forming sequence. The results of our simulations shed light on the factors leading to an ordered secondary structure in a model peptide: in particular, the importance of the so-called diagonal interactions in forming a stable hydrophobic nucleus in the beta-hairpin, together with the more obvious lateral interactions, is examined. With the use of long timescale MD simulations in explicit water, we show the role of diagonal interactions in driving the peptide to the correct folded structure (formation of the hydrophobic core with Trp 2, Tyr 4, and Phe 9 in the first stages of refolding) and in keeping it in the ensemble of

SUBMITTER: Colombo G 

PROVIDER: S-EPMC2312445 | biostudies-literature | 2003 Mar

REPOSITORIES: biostudies-literature