Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Relating protein motion to catalysis.

Sharon Hammes-Schiffer1, Stephen J Benkovic

  • 1Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, USA. shs@chem.psu.edu

Annual Review of Biochemistry
|June 8, 2006
PubMed
Summary

Protein motions are crucial for enzyme catalysis. This review highlights how coupled protein dynamics in enzymes like dihydrofolate reductase facilitate hydride transfer reactions through coordinated conformational changes.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Protein-Solvent Interface Controls Proton-Coupled Reactivity in Cryptochrome 4a.

Journal of the American Chemical Society·2026
Same author

Extended Lagrangian molecular dynamics on vibronic surfaces in the nuclear-electronic orbital framework.

The Journal of chemical physics·2026
Same author

General Expression for Vibronic Coupling in Proton-Coupled Energy Transfer.

Journal of chemical theory and computation·2026
Same author

Capturing nuclear quantum effects in high-pressure superconducting hydrides and ice with nuclear-electronic orbital theory.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Proton-Coupled Electron and Energy Transfer in Molecular Triads.

Accounts of chemical research·2026
Same author

Nuclear-electronic orbital quasiclassical trajectory method for vibrational spectroscopy.

The Journal of chemical physics·2026

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Enzyme catalysis is a complex process involving intricate protein structures.
  • Understanding the role of protein dynamics in enzyme function is essential for deciphering reaction mechanisms.

Purpose of the Study:

  • To review the relationship between protein conformational motions and enzyme catalysis.
  • To investigate this linkage using dihydrofolate reductase and liver alcohol dehydrogenase as models for hydride transfer enzymes.

Main Methods:

  • Summary of extensive experimental studies.
  • Analysis of theoretical investigations.
  • Focus on enzymes catalyzing hydride transfer.

Main Results:

  • Evidence for a network of coupled motions throughout the protein fold.
  • Identification of fast thermal motions in equilibrium with the reaction coordinate.
  • Observation of slower equilibrium conformational changes that favor the chemical reaction.

Conclusions:

  • Protein conformational dynamics are intrinsically linked to enzyme catalysis.
  • A network of coupled motions, including both fast and slow components, facilitates hydride transfer reactions.
  • These dynamics are essential for optimizing the enzyme's catalytic efficiency.

Related Experiment Videos