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PMID: 10908712 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Substrate binding and enzyme function investigated by infrared spectroscopy.

FEBS letters ·Vol. 477 ·No. 3 ·2000-07-21 ·Pages 151-6

Barth A, Zscherp C

Abstract

Protein conformational changes triggered by molecule binding are increasingly investigated by infrared spectroscopy often using caged compounds. Several examples of molecule-protein recognition studies are given, which focus on nucleotide binding to proteins. The investigation of enzyme mechanisms is illustrated in detail using the Ca(2+)-ATPase of the sarcoplasmic reticulum membrane as an example. It is shown that infrared spectroscopy provides valuable information on general aspects of enzyme function as well as on molecular details of molecule-protein interactions and the mechanism of catalysis.

MeSH Terms
Calcium-Transporting ATPases/metabolism Sarcoplasmic Reticulum/enzymology Spectrophotometry, Infrared Substrate Specificity
Chemicals
Calcium-Transporting ATPases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Barth A
Institut für Biophysik, Johann Wolfgang Goethe-Universität, Theodor-Stern-Kai 7, Haus 74, D-60590, Frankfurt am Main, Germany. barth@biophysik.uni-frankfurt.de
Zscherp C
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2000-07-21
Pages
151-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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