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Global conformations of proteins as predicted from the modeling of their CZE mobility data
Author(s) -
Deiber Julio A.,
Piaggio María V.,
Peirotti Marta B.
Publication year - 2011
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.201100016
Subject(s) - chemistry , scaling , hydrodynamic radius , chemical physics , radius , biological system , protein structure , amino acid residue , radius of gyration , peptide sequence , aqueous solution , biochemistry , mathematics , computer science , polymer , geometry , computer security , micelle , biology , organic chemistry , gene
Abstract Estimations of protein global conformations in well‐specified physicochemical microenvironments are obtained through global structural parameters defined from polypeptide‐scale analyses. For this purpose protein electrophoretic mobility data must be interpreted through a physicochemical CZE model to obtain estimates of protein equivalent hydrodynamic radius, effective and total charge numbers, hydration, actual ionizing pK and pH‐near molecule. The electrical permittivity of protein domain is also required. In this framework, the solvent drag on proteins is obtained via the characteristic friction power coefficient associated with the number of amino acid residues defining the global chain conformation in solution. Also, the packing dimension related to the spatial distribution of amino acid residues within the protein domain is evaluated and discussed. These scaling coefficients together with the effective and total charge number fractions of proteins provide relevant interpretations of protein global conformations mainly from collapsed globule to hybrid chain regimes. Also, protein transport properties may be estimated within this framework. In this regard, the central role played by the friction power coefficient in the evaluation of these properties is highlighted.