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Article

Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase.

Biochemistry - 26 Mar 2013

Fan Yao, Cembran Alessandro, Ma Shuhua, Gao Jiali

Abstract excerpt

Combined quantum mechanics/molecular mechanics molecular dynamics simulations reveal that the M20 loop conformational dynamics of dihydrofolate reductase (DHFR) is severely restricted at the transition state of the hydride transfer as a result of the M42W/G121V double mutation. Consequently, the double-mutant enzyme has a reduced entropy of activation, i.e., increased entropic barrier, and altered temperature...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 23297871
DOI: 10.1021/bi301559q
PMCID: PMC3773050

Genes

DHFR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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