ISSN:
0749-1581
Keywords:
Nuclear magnetic resonance
;
Renin inhibitor peptide
;
Nuclear Overhauser effect
;
Correlated spectroscopy
;
Mixing time
;
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
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-d6 using 2D NMR techniques. Some of the backbone NH protons show a very low temperature coefficient, indicating their involvement in intramolecular hydrogen bonding. The 3J(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.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/mrc.1260270507
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