An NMR perspective on enzyme dynamics

David D. Boehr, H. Jane Dyson, Peter E. Wright

Research output: Contribution to journalArticlepeer-review

337 Scopus citations

Abstract

Nuclear magnetic resonance (NMR) relaxation techniques have proved effective in the study of multiple time-scale dynamics of enzymes in different phases of the catalytic cycle. Some of the documented studies using NMR in enzyme dynamics include conformational selection in ribonuclease A, reaction of coordinate compression in E. coli dihydrofolate reductase, substrate binding and drug resistance in HIV protease, protein dynamics during turnover in cyclophilin A and mesophilic and thermophilic enzymes. In all these applications, NMR showed that protein motion plays important roles in all aspects of catalysis.

Original languageEnglish (US)
Pages (from-to)3055-3079
Number of pages25
JournalChemical Reviews
Volume106
Issue number8
DOIs
StatePublished - Aug 2006

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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