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Article

Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.

Proceedings of the National Academy of Sciences of the United States of America - 24 Oct 2006

Wang Lin, Goodey Nina M, Benkovic Stephen J, Kohen Amnon

Abstract excerpt

One of the most intriguing questions in modern enzymology is whether enzyme dynamics evolved to enhance the catalyzed chemical transformation. In this study, dihydrofolate reductase, a small monomeric protein that catalyzes a single C-H-C transfer, is used as a model system to address this question. Experimental and computational studies have proposed a dynamic network that includes two residues remote from the...

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Identifiers

PMID: 17032759
DOI: 10.1073/pnas.0606976103
PMCID: PMC1635075

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.PMID 17032759Read ↗

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Simulations of remote mutants of dihydrofolate reductase reveal the nature of a network of residues coupled to hydride transfer.Semantic proximity Read ↗

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Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase.Semantic proximity Read ↗

Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase.Semantic proximity Read ↗

Correlated motion and the effect of distal mutations in dihydrofolate reductase.Semantic proximity Read ↗

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