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Updated: May 21, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

An outer membrane protein undergoes enthalpy- and entropy-driven transitions.

Belete R Cheneke1, Mridhu Indic, Bert van den Berg

  • 1Department of Physics, Syracuse University, 201 Physics Building, Syracuse, NY 13244-1130, USA.

Biochemistry
|June 12, 2012
PubMed
Summary

Outer membrane carboxylate channels like OccK1 exhibit complex gating dynamics with both enthalpy-driven and entropy-driven transitions. Temperature influences the most favorable open state, revealing distinct functional traits of beta-barrel proteins.

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