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Observation of a tight‐turn conformation in a proline‐containing inhibitor of renin angiotensin
Author(s) -
Srivastava Sudha,
Phadke Ratna S.,
Govil Girjesh
Publication year - 1989
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.1260270507
Subject(s) - chemistry , intramolecular force , salt bridge , hydrogen bond , proton magnetic resonance , residue (chemistry) , turn (biochemistry) , peptide , proline , crystallography , proton , proton nmr , molecule , chemical shift , stereochemistry , nuclear magnetic resonance , organic chemistry , amino acid , biochemistry , physics , quantum mechanics , mutant , gene
The solution conformation of renin inhibitor peptide, Pro‐His‐Pro‐Phe‐His‐Phe‐Phe‐Val‐Tyr‐Lys, was established using proton magnetic resonance techniques. As a first step a complete resonance assignment was made in DMSO‐ d 6 using 2D NMR techniques. Some of the backbone NH protons show a very low temperature coefficient, indicating their involvement in intramolecular hydrogen bonding. The 3 J (NH–Cα, H) values the inter‐residue NOEs, the temperature coefficient of the backbone NH protons and the chemical shift positions indicate the presence of a tight turn in the molecule. A model is proposed, using computer graphics, based on the experimental results.