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- Title
Nascent helix in the multiphosphorylated peptide α<sub>S2</sub>-casein(220).
- Authors
N. Laila Huq; Keith J. Cross; Eric C. Reynolds
- Abstract
Sequence-specific nuclear magnetic resonance (NMR) assignments have been determined for the peptide αS2-CN(220) containing the multiphosphorylated motif-8Ser(P)-Ser(P)-Ser(P)-Glu-Glu12- in the presence of molar excess Ca2+. The secondary structure of the peptide was characterized by sequential (i,i + 1), medium-range (i,i + 2/3/4) nOes and Hα chemical shifts. Molecular modelling of the peptide based on these constraints suggests a nascent helix for residues Ser(P)9 to Glu12. The spectral data for αS2-CN(220) were compared with those of other casein phosphopeptides β-CN(125) and αS1-CN(5979) that also contain the multiphosphorylated motif. This comparison revealed a similar pattern of secondary amide chemical shifts in the multiphosphorylated motif. However, the patterns of medium-range nOe connectivities in the three peptides suggests they have distinctly different conformations in the presence of Ca2+ despite having a high degree of sequential similarity. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.
- Subjects
PEPTIDES; NUCLEAR magnetic resonance; CONFORMATIONAL analysis; AMINO acid sequence; CASEINS; CALCIUM ions; AMIDES
- Publication
Journal of Peptide Science, 2003, Vol 9, Issue 6, p386
- ISSN
1075-2617
- Publication type
Article
- DOI
10.1002/psc.465