Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS.

Abstract:

: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.

authors

Gudiksen KL,Gitlin I,Whitesides GM

doi

10.1073/pnas.0602816103

subject

Has Abstract

pub_date

2006-05-23 00:00:00

pages

7968-72

issue

21

eissn

0027-8424

issn

1091-6490

pii

0602816103

journal_volume

103

pub_type

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