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Article

Conformational preferences underlying reduced activity of a thermophilic ribonuclease H.

Journal of molecular biology - 27 Feb 2015

Stafford Kate A, Trbovic Nikola, Butterwick Joel A, Abel Robert, Friesner Richard A, Palmer Arthur G

Abstract excerpt

The conformational basis for reduced activity of the thermophilic ribonuclease HI enzyme from Thermus thermophilus, compared to its mesophilic homolog from Escherichia coli, is elucidated using a combination of NMR spectroscopy and molecular dynamics (MD) simulations. Explicit-solvent all-atom MD simulations of the two wild-type proteins and an E. coli mutant in which a glycine residue is inserted after position...

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Source

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Identifiers

PMID: 25550198
DOI: 10.1016/j.jmb.2014.11.023
PMCID: PMC4349505

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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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