Temporally overlapped but uncoupled motions in dihydrofolate reductase catalysis

C. Tony Liu, Lin Wang, Nina M. Goodey, Philip Hanoian, Stephen J. Benkovic

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Temporal correlations between protein motions and enzymatic reactions are often interpreted as evidence for catalytically important motions. Using dihydrofolate reductase as a model system, we show that there are many protein motions that temporally overlapped with the chemical reaction, and yet they do not exhibit the same kinetic behaviors (KIE and pH dependence) as the catalyzed chemical reaction. Thus, despite the temporal correlation, these motions are not directly coupled to the chemical transformation, and they might represent a different part of the catalytic cycle or simply be the product of the intrinsic flexibility of the protein.

Original languageEnglish (US)
Pages (from-to)5332-5334
Number of pages3
Issue number32
StatePublished - Aug 13 2013

All Science Journal Classification (ASJC) codes

  • Biochemistry


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