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Conformation of renin substrate (angiotensinogen) in water is different from DMSO: a 1 H NMR and molecular dynamics study
Author(s) -
Patel Anant B.,
Srivastava Sudha,
Phadke Ratna S.,
Coutinho Evans,
Kamath Shantaram
Publication year - 1998
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/(sici)1097-458x(199804)36:4<285::aid-omr247>3.0.co;2-8
Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , molecular dynamics , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , nmr spectra database , crystallography , substrate (aquarium) , aqueous solution , spectral line , computational chemistry , physics , astronomy , oceanography , geology
The conformation of angiotensinogen, a tetradecapeptide, with the sequence Asp1–Arg2–Val3–Tyr4–Ile5–His6–Pro7–Phe8–His9–Leu10–Leu11–Val12–Tyr13–Ser14, was studied in aqueous medium by 2D NMR spectroscopy. Complete resonance assignments were made using a combination of DQF‐COSY, TOCSY and NOESY spectra. The kinetics of deuterium exchange of NH protons were also studied. The NMR results indicate the presence of at least two conformations in dynamic equilibrium. A total of 39 NOEs were used in the restrained molecular dynamics simulation to generate the solution structure. The dominant conformation of angiotensinogen is characterized by a β‐turn around the tetrapeptide sequence Val3–Tyr4–Ile5–His6, two γ‐bends at Tyr4 and Leu10 and a sharp turn around Val12. The conformation of angiotensinogen in water is radically different from the conformation in DMSO reported earlier. ©1998 John Wiley & Sons, Ltd.