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Analysis of the interplay among charge, hydration and shape of proteins through the modeling of their CZE mobility data
Author(s) -
Piaggio Maria V.,
Peirotti Marta B.,
Deiber Julio A.
Publication year - 2009
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200800743
Subject(s) - fractal dimension , hydrodynamic radius , chemical physics , electrophoresis , chemistry , radius , diffusion , fractal , charge (physics) , shape factor , thermodynamics , chromatography , physics , geometry , mathematics , computer security , quantum mechanics , aqueous solution , computer science , micelle , mathematical analysis
Electrophorectic mobility data of four proteins are analyzed and interpreted through a physicochemical CZE model, which provides estimates of quantities like equivalent hydrodynamic radius (size), effective charge number, shape orientation factor, hydration, actual p K values of ionizing groups, and pH near molecule, among others. Protein friction coefficients are simulated through the creeping flow theory of prolate spheroidal particles. The modeling of the effective electrophoretic mobility of proteins requires consideration of hydrodynamic size and shape coupled to hydration and effective charge. The model proposed predicts native protein hydrations within the range of values obtained experimentally from other techniques. Therefore, this model provides consistently other physicochemical properties such as average friction and diffusion coefficients and packing fractal dimension. As the pH varies from native conditions to those that are denaturing the protein, hydration and packing fractal dimension change substantially. Needs for further research are also discussed and proposed.