Phosphorus nuclear-magnetic-resonance studies of a transition-state analogue complex of creatine kinase

Milner-White, E. J. and Rycroft, D. S. (1977) Phosphorus nuclear-magnetic-resonance studies of a transition-state analogue complex of creatine kinase. Biochemical Journal : Molecular Aspects, 167(3), pp. 827-829. (doi:10.1042/bj1670827) (PMID:603637)

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Abstract

31P nuclear-magnetic-resonance spectra of MgADP bound to creatine kinase in the presence of creatine NO3 ions show that there are two non-identical forms of the bound nucleotide. The sites have different affinities for the nucleotide. MgADP at the high-affinity site is in slow exchange (k <125s−1 at 27°C) with free MgADP.

Item Type:Articles
Keywords:NMR spectroscopy, phosphorus chemistry.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Rycroft, Dr David and Milner-White, Professor E
Authors: Milner-White, E. J., and Rycroft, D. S.
Subjects:Q Science > QD Chemistry
Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Science and Engineering > School of Chemistry
College of Medical Veterinary and Life Sciences > School of Life Sciences
Journal Name:Biochemical Journal : Molecular Aspects
Journal Abbr.:Biochem. J.
Publisher:Portland Press Ltd.
ISSN:0306-3275

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