NMR evidence for the nucleation of a β-hairpin peptide conformation in water by an Asn-Gly type I′ β-turn sequence

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Abstract
The contribution of the β-turn sequence to the folding and stability of a peptide β-hairpin in water has been analysed from studies of a truncated peptide lacking one β-strand and hence the majority of the interstrand hydrophobic interactions; NMR analysis shows that the Asn-Gly type I′ β-turn conformation is significantly populated, suggesting that the intrinsic conformation preference of the turn sequence may play an important role in nucleating hairpin folding.

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