Aj. Maynard et Ms. Searle, NMR STRUCTURAL-ANALYSIS OF A BETA-HAIRPIN PEPTIDE DESIGNED FOR DNA-BINDING, Chemical communications, (14), 1997, pp. 1297-1298
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.