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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Updated: May 27, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Dynamic light scattering to study allosteric regulation.

Aaron L Lucius¹, P Keith Veronese, Ryan P Stafford

¹Department of Chemistry, The University of Alabama at Birmingham, Birmingham, AL, USA. allucius@uab.edu

Methods in Molecular Biology (Clifton, N.J.)

|November 5, 2011

Summary

We developed a new method using dynamic light scattering (DLS) to precisely measure diffusion coefficients. This technique, combined with analytical ultracentrifugation, enhances understanding of Escherichia coli ClpA protein assembly and nucleotide binding regulation.

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Escherichia coli ClpA protein is an AAA+ motor protein.
AAA+ motor proteins are allosterically regulated by nucleotide binding.

Purpose of the Study:

To examine the self-association properties of E. coli ClpA.
To investigate the allosteric linkage of assembly to nucleotide binding.
To present a protocol for rapid and precise diffusion coefficient determination using DLS.

Main Methods:

Analytical ultracentrifugation
Dynamic Light Scattering (DLS)
Model-independent diffusion coefficient determination

Main Results:

A protocol for rapid and precise diffusion coefficient determination using DLS was developed.
The combined approach provides a more complete understanding of hydrodynamic and thermodynamic properties.

Conclusions:

The new DLS protocol, when used with analytical ultracentrifugation, offers a powerful method to study AAA+ motor protein regulation.
This approach enhances the understanding of allosteric regulation in proteins like E. coli ClpA.