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Article

NMR investigation of Tyr105 mutants in TEM-1 beta-lactamase: dynamics are correlated with function.

The Journal of biological chemistry - 20 Jul 2007

Doucet Nicolas, Savard Pierre-Yves, Pelletier Joelle N, Gagné Stéphane M

Abstract excerpt

The existence of coupled residue motions on various time scales in enzymes is now well accepted, and their detailed characterization has become an essential element in understanding the role of dynamics in catalysis. To this day, a handful of enzyme systems has been shown to rely on essential residue motions for catalysis, but the generality of such phenomena remains to be elucidated. Using NMR spectroscopy, we...

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PMID: 17426035
DOI: 10.1074/jbc.M609777200

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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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