NMR evidence for the nucleation of a β-hairpin peptide conformation in water by an Asn-Gly type I′ β-turn sequence
1998; Royal Society of Chemistry; Issue: 7 Linguagem: Inglês
10.1039/a800749g
ISSN1364-548X
AutoresSam Griffiths‐Jones, Allister J. Maynard, Gary J. Sharman,
Tópico(s)RNA and protein synthesis mechanisms
ResumoThe 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.
Referência(s)