NMR STRUCTURAL-ANALYSIS OF A BETA-HAIRPIN PEPTIDE DESIGNED FOR DNA-BINDING

Citation
Aj. Maynard et Ms. Searle, NMR STRUCTURAL-ANALYSIS OF A BETA-HAIRPIN PEPTIDE DESIGNED FOR DNA-BINDING, Chemical communications, (14), 1997, pp. 1297-1298
Citations number
26
Categorie Soggetti
Chemistry
Journal title
ISSN journal
13597345
Issue
14
Year of publication
1997
Pages
1297 - 1298
Database
ISI
SICI code
1359-7345(1997):14<1297:NSOABP>2.0.ZU;2-U
Abstract
NMR and circular dichroism (CD) spectroscopy shows that an unconstrain ed 16 residue linear peptide folds autonomously in water into a beta-h airpin: the designed peptide adopts a conformation that mimics the ant i-parallel beta-sheet DNA binding motif of the met repressor protein d imer with key residues for DNA recognition presented in the same posit ions and orientations principally on one face of the beta-hairpin temp late.