Atomic motion in enzymatic reaction coordinates

Vern L. Schramm, Wuxian Shi

Research output: Contribution to journalReview articlepeer-review

63 Scopus citations


Atomic excursions of reactants in enzymatic catalytic sites can be estimated from high-resolution crystal structures of enzyme complexes with substrates, transition state analog inhibitors and products. Transition state structures, defined from kinetic isotope effect studies, are compared to crystallographic structures to validate the properties of the transition state analog. Atomic excursions in enzymatic catalytic sites can differ from those in solution and define the role of the enzymatic catalyst in directing atomic motion.

Original languageEnglish (US)
Pages (from-to)657-665
Number of pages9
JournalCurrent Opinion in Structural Biology
Issue number6
StatePublished - Dec 1 2001

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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