A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.

Abstract

Proton NMR has been used to study a site-directed mutant of yeast phosphoglycerate kinase in which the interdomain residue His388 has been replaced by a glutamine residue. Using 1H-NMR spectroscopy, it was found that 3-phosphoglycerate binding to the mutant protein induces different conformational effects to those observed for the wild-type enzyme. These… (More)

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Cite this paper

@article{Graham1991APS, title={A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.}, author={Hannah Graham and R. J. Williams and Jennifer A. Littlechild and H. C. Watson}, journal={European journal of biochemistry}, year={1991}, volume={196 2}, pages={261-9} }