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Article

Site-Specific Tryptophan Labels Reveal Local Microsecond-Millisecond Motions of Dihydrofolate Reductase.

Molecules (Basel, Switzerland) - 22 Aug 2020

Vaughn Morgan B, Biren Chloe, Li Qun, Ragupathi Ashwin, Dyer R Brian

Abstract excerpt

Many enzymes are known to change conformations during their catalytic cycle, but the role of these protein motions is not well understood. Escherichia coli dihydrofolate reductase (DHFR) is a small, flexible enzyme that is often used as a model system for understanding enzyme dynamics. Recently, native tryptophan fluorescence was used as a probe to study micro- to millisecond dynamics of DHFR. Yet, because DHFR...

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Identifiers

PMID: 32842574
DOI: 10.3390/molecules25173819
PMCID: PMC7503464

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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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