Study of the electrostatic effects of mutations on the surface of dehaloperoxidase-hemoglobin A
Zhao, J., Rowe, J., Franzen, J., He, C., & Franzen, S. (2012, March 17). Biochemical and Biophysical Research Communications, Vol. 420, pp. 733–737.
author keywords: Surface mutation; Electrostatic interaction; Isoelectric focusing; Ionic strength effect; Enzyme kinetics
MeSH headings : Animals; Hemoglobin A / chemistry; Hemoglobin A / genetics; Mutagenesis; Mutation; Peroxidases / chemistry; Peroxidases / genetics; Polychaeta / enzymology; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Static Electricity
topics (OpenAlex): Hemoglobin structure and function; Erythrocyte Function and Pathophysiology; Chemical and Physical Studies
TL;DR:
The electrostatic nature of substrate binding was further confirmed by the result that kinetic assays of DHP A were affected by ionic strength, and isoelectric focusing gel study showed that D HP A has a slight negative charge pH 7, consistent with the kinetic observations.
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