Abstract
NMR and circular dichroism (CD) spectroscopy shows that an unconstrained 16 residue linear peptide folds autonomously in water into a β-hairpin: the designed peptide adopts a conformation that mimics the anti-parallel β-sheet DNA binding motif of the met repressor protein dimer with key residues for DNA recognition presented in the same positions and orientations principally on one face of the β-hairpin template.
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