Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS
Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS
Published online before print May 12, 2006
Katherine L. Gudiksen, Irina Gitlin, and George M. Whitesides*
PNAS
Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138
This paper shows that proteins display an unexpectedly wide range of behaviors in buffers containing moderate (0.1?10 mM) concentrations of SDS (complete unfolding, formation of stable intermediate states, specific association with SDS, and various kinetic phenomena); capillary electrophoresis provides a convenient method of examining these behaviors. Examination of the dynamics of the response of proteins to SDS offers a way to differentiate and characterize proteins. Based on a survey of 18 different proteins, we demonstrate that proteins differ in the concentrations of SDS at which they denature, in the rates of unfolding in SDS, and in the profiles of the denaturation pathways. We also demonstrate that these differences can be exploited in the analysis of mixtures.
capillary electrophoresis | surfactant | intermediates | kinetics
Contributed by George M. Whitesides, April 6, 2006
Author contributions: K.L.G. and G.M.W. designed research; K.L.G. and I.G. performed research; K.L.G. and I.G. analyzed data; and K.L.G., I.G., and G.M.W. wrote the paper.
Conflict of interest statement: No conflicts declared.
*To whom correspondence should be addressed. E-mail: gwhitesides@gmwgroup.harvard.edu
? 2006 by The National Academy of Sciences of the USA
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