title: Dynamic light scattering to study allosteric regulation.
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.
authors: Department of Chemistry, The University of Alabama at Birmingham, Birmingham, AL, USA. allucius@uab.edu
authors: Aaron L
authors: AL
authors: Lucius
authors: P Keith
authors: PK
authors: Veronese
authors: Ryan P
authors: RP
authors: Stafford
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology; D049071:Endopeptidase Clp / Q000737:chemistry* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D008027:Light; D011487:Protein Conformation; D012542:Scattering, Radiation; D013816:Thermodynamics; D014461:Ultracentrifugation / Q000379:methods
chemical_list: D029968:Escherichia coli Proteins; C483568:ClpA protease, E coli; D049071:Endopeptidase Clp