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Conformational heterogeneity in polypeptide cardiac stimulants from sea anemones
Author(s) -
Gooley Paul R.,
Blunt John W.,
Norton Raymond S.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81068-6
Subject(s) - chemistry
High‐resolution 1 H NMR spectra at 300 MHz of the polypeptide cardiac stimulants anthopIeurin‐A and Anemonia sulcata toxin II reveal conformational heterogeneity in both molecules. The two conformations, manifest in a number of split 1 H resonances, are in slow exchange over a wide range of pH and temperature. Heterogeneity affects a region of these molecules containing the structurally and functionally important Asp residues. By comparison with a homologous polypeptide Anemonia sulcata toxin I, which does not show this type of heterogeneity, it is suggested that the heterogeneity may originate in cis‐trans isomerism of the Gly‐40 to Pro‐41 peptide bond.