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Related Experiment Video

Updated: Feb 15, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Engineered control of enzyme structural dynamics and function.

David D Boehr¹, Rebecca N D'Amico¹, Kathleen F O'Rourke¹

¹Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802, USA.

Protein Science : a Publication of the Protein Society

|January 31, 2018

Summary

This summary is machine-generated.

Enzymes

Keywords:

allostery enzyme catalysis external stimulus networks protein dynamics protein engineering stimulus-responsive material structural dynamics

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Area of Science:

Biochemistry and Molecular Biology
Enzyme Engineering

Background:

Enzymes exhibit dynamic internal motions crucial for their function, including catalysis and ligand interactions.
Protein engineering and post-translational modifications offer methods to control enzyme dynamics.

Purpose of the Study:

To explore the functional significance of enzyme structural dynamics.
To investigate methods for engineering enzymes with controlled conformational changes.
To develop stimulus-responsive enzymes for biotechnological applications.

Main Methods:

Protein engineering approaches targeting specific amino acid interactions.
Creation of chimeric enzymes with novel regulatory functions.
Investigating post-translational covalent modifications for enzyme control.

Main Results:

Demonstrated insights into the functional roles of protein motions.
Engineering of enzymes to respond to external stimuli like light and pH.
Development of novel allosteric modulators for enzyme control.

Conclusions:

Controlling enzyme structural dynamics offers new tools for biotechnology and medicine.
Engineered enzymes can be made stimulus-responsive.
Understanding protein motions is key to enzyme function and engineering.