| Literature DB >> 2720088 |
J Burton1, S G Wood, A Pedyczak, I Z Siemion.
Abstract
The mean solution conformation of tetrapeptide fragments of the hinge region of human IgA1 molecule was investigated by CD and 13C-NMR methods. Distinct conformational differences for the partial sequences were found. Tetrapeptides with the Thr-Pro-Ser-Pro sequence were found to show a clear preference for the beta-turn conformation. Conformational equilibria of these peptides are only slightly affected by acetylation or pH changes. In the case of Pro-Thr-Pro-Ser tetrapeptides conformational equilibria are dominated by unordered forms.Entities:
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Year: 1989 PMID: 2720088 DOI: 10.1016/0301-4622(89)80005-5
Source DB: PubMed Journal: Biophys Chem ISSN: 0301-4622 Impact factor: 2.352