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Updated: Apr 15, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Protein motions and dynamic effects in enzyme catalysis
Louis Y P Luk1, E Joel Loveridge1, Rudolf K Allemann1
1School of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK. allemannrk@cardiff.ac.uk.
Protein dynamics can hinder enzyme catalysis, suggesting evolutionary selection against such motions in dihydrofolate reductase (DHFR). Fine-tuning protein movements is crucial for optimal enzyme function.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- The precise role of protein dynamics in enzyme catalysis is debated.
- Dihydrofolate reductase (DHFR) is a key enzyme in folate metabolism.
Purpose of the Study:
- To provide a unified view of protein dynamics in DHFR catalysis.
- To investigate how protein motions influence the chemical step of enzymatic reactions.
Main Methods:
- Characterization of biophysical properties of isotopically substituted DHFR.
- Combination of experimental and computational analyses.
Main Results:
- Dynamic coupling to the chemical coordinate appears detrimental to catalysis.
- Evidence suggests evolutionary selection against specific protein motions in DHFR.
Conclusions:
- Protein dynamics play a complex role in enzyme catalysis, with some motions being disadvantageous.
- Optimal enzyme catalysis relies on the precise regulation of protein motions throughout the catalytic cycle.
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