2012 journal article

Study of the electrostatic effects of mutations on the surface of dehaloperoxidase-hemoglobin A


By: J. Zhao n, J. Rowe n, J. Franzen n, C. He* & S. Franzen n

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
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. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.