Abstract
Sensitive yet selective techniques for characterizing protein unfolding are important for assessing the conformational stability of wild-type and recombinant protein. This review presents a summary of recent developments in protein unfolding by capillary electrophoresis (CE). Relative to conventional spectroscopic methods, CE offers a versatile microseparation format for performing unfolding studies using small amounts of protein mixtures based on thermal or chemical denaturation. The fundamental theory of protein unfolding in CE, as well as correction factors required to normalize non-specific changes in apparent mobility are examined in this review. The integration of in-capillary ligand stripping with dynamic protein unfolding by CE provides a convenient way to characterize holoproteins without sample pretreatment. CE is also a useful format for resolving protein conformational intermediates involving multimeric proteins or oligomers that is relevant to understanding the dynamics of misfolded proteins. This review covers protein unfolding and conformational studies from 1991-2006 with emphasis on recent developments in CE that highlight its significance as a complementary biophysical tool for protein characterization.
Keywords: Protein unfolding, Conformational intermediates, Thermodynamics, Kinetics, Capillary Electrophoresis, Review
Current Analytical Chemistry
Title: Protein Unfolding and Conformational Studies by Capillary Electrophoresis
Volume: 3 Issue: 1
Author(s): Jennilee M.A. Gavina and Philip Britz-McKibbin
Affiliation:
Keywords: Protein unfolding, Conformational intermediates, Thermodynamics, Kinetics, Capillary Electrophoresis, Review
Abstract: Sensitive yet selective techniques for characterizing protein unfolding are important for assessing the conformational stability of wild-type and recombinant protein. This review presents a summary of recent developments in protein unfolding by capillary electrophoresis (CE). Relative to conventional spectroscopic methods, CE offers a versatile microseparation format for performing unfolding studies using small amounts of protein mixtures based on thermal or chemical denaturation. The fundamental theory of protein unfolding in CE, as well as correction factors required to normalize non-specific changes in apparent mobility are examined in this review. The integration of in-capillary ligand stripping with dynamic protein unfolding by CE provides a convenient way to characterize holoproteins without sample pretreatment. CE is also a useful format for resolving protein conformational intermediates involving multimeric proteins or oligomers that is relevant to understanding the dynamics of misfolded proteins. This review covers protein unfolding and conformational studies from 1991-2006 with emphasis on recent developments in CE that highlight its significance as a complementary biophysical tool for protein characterization.
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Cite this article as:
Gavina M.A. Jennilee and Britz-McKibbin Philip, Protein Unfolding and Conformational Studies by Capillary Electrophoresis, Current Analytical Chemistry 2007; 3 (1) . https://dx.doi.org/10.2174/157341107779314208
DOI https://dx.doi.org/10.2174/157341107779314208 |
Print ISSN 1573-4110 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6727 |
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