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Protein motions and dynamic effects in enzyme catalysis

Luk, Louis Yu Pan, Loveridge, Edric Joel and Allemann, Rudolf Konrad 2015. Protein motions and dynamic effects in enzyme catalysis. Physical Chemistry Chemical Physics 17 , pp. 30817-30827. 10.1039/C5CP00794A

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Abstract

The role of protein motions in promoting the chemical step of enzyme catalysed reactions remains a subject of considerable debate. Here, a unified view of the role of protein dynamics in dihydrofolate reductase catalysis is described. Recently the role of such motions has been investigated by characterising the biophysical properties of isotopically substituted enzymes through a combination of experimental and computational analyses. Together with previous work, these results suggest that dynamic coupling to the chemical coordinate is detrimental to catalysis and may have been selected against during DHFR evolution. The full catalytic power of Nature's catalysts appears to depend on finely tuning protein motions in each step of the catalytic cycle.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Subjects: Q Science > QD Chemistry
Publisher: Royal Society of Chemistry
ISSN: 1463-9076
Funders: BBSRC
Date of First Compliant Deposit: 30 March 2016
Date of Acceptance: 30 March 2015
Last Modified: 05 Jun 2017 04:56
URI: http://orca.cf.ac.uk/id/eprint/73319

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Cited 18 times in Scopus. View in Scopus. Powered By Scopus® Data

Cited 2 times in Web of Science. View in Web of Science.

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