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Literature DB >> 20338851

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

Amy D Hanlon¹, Michael I Larkin, Ryan M Reddick.

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.

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Year: 2010 PMID： 20338851 PMCID： PMC2808485 DOI： 10.1016/j.bpj.2009.09.061

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

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