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Article

Enzyme-Substrate-Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry.

Biochemistry - 30 Jun 2020

Rosenberg Masha M, Yao Tianjiong, Patton Gregory C, Redfield Alfred G, Roberts Mary F, Hedstrom Lizbeth

Abstract excerpt

The remarkable power and specificity of enzyme catalysis rely on the dynamic alignment of the enzyme, substrates, and cofactors, yet the role of dynamics has usually been approached from the perspective of the protein. We have been using an underappreciated NMR technique, subtesla high-resolution field cycling 31P NMR relaxometry, to investigate the dynamics of the enzyme-bound substrates and cofactor on...

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PMID: 32479091
DOI: 10.1021/acs.biochem.0c00212
PMCID: PMC8364753

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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