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Loss in conformational rigidity of bradykinin on replacement of the Phe‐8 by tyrosine
Author(s) -
Srivastava Sudha,
Haram S.,
Phadke Ratna S.
Publication year - 1991
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260290409
Subject(s) - chemistry , bradykinin , rigidity (electromagnetism) , chemical shift , tyrosine , peptide , structural rigidity , coupling constant , stereochemistry , crystallography , nuclear magnetic resonance spectroscopy , biochemistry , receptor , physics , geometry , mathematics , structural engineering , particle physics , engineering
The complete resonance assignments and the conformation of the hormone [Tyr 8 ]‐bradykinin, a nonapeptide, in DMSO‐ d 6 have been determined using 2D 1 H NMR techniques. NMR parameters such as the chemical shifts, coupling constants, temperature coefficients of the backbone NH protons and NOEs have been analysed in the light of the known conformation of the native peptide. The results indicate that the peptide loses conformational rigidity on the replacement of Phe‐8 by Tyr.