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Biophys J. 2010 Jan 20;98(2):297-304. doi: 10.1016/j.bpj.2009.09.061.

Free-solution, label-free protein-protein interactions characterized by dynamic light scattering.

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  • 1Department of Research and Development, Wyatt Technology, Santa Barbara, California, USA. ahanlon@wyatt.com

Abstract

We report a free-solution, label-free method for quantitative characterization of macromolecular interactions using dynamic light scattering, a temperature controlled plate reader, and a multiwell concentration gradient. This nondestructive technique enabled determination of stoichiometry of binding, equilibrium dissociation constant, and thermodynamic parameters, as well as the impact of temperature, buffer salinity, and a small-molecule inhibitor. The low volume capability of dynamic light scattering reduced the required sample to 426 pmol/experiment, with detection limits for 150-kDa proteins anticipated to be in the low femtomole range.

Copyright 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.

PMID:
20338851
[PubMed - indexed for MEDLINE]
PMCID:
PMC2808485
Free PMC Article
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