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Methods Mol Biol. 2012;796:175-86. doi: 10.1007/978-1-61779-334-9_9.

Dynamic light scattering to study allosteric regulation.

Author information

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

Abstract

The Escherichia coli ClpA protein, like many AAA+ motor proteins, is allosterically regulated by nucleotide binding. We have combined analytical ultracentrifugation approaches with dynamic light scattering (DLS) to examine the self-association properties and the allosteric linkage of assembly to nucleotide binding. Here we present a protocol for the rapid and precise determination of the diffusion coefficient using DLS measurements in a model-independent fashion. When combined with analytical ultracentrifugation experiments, such an approach can yield a more complete understanding of the hydrodynamic and thermodynamic properties of the system.

PMID:
22052490
DOI:
10.1007/978-1-61779-334-9_9
[Indexed for MEDLINE]

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