Structural features important for differences in protein partitioning in aqueous dextran-polyethylene glycol two-phase systems of different ionic compositions
authors Ferreira, L; Fan, X; Mikheeva, LM; Madeira, PP; Kurgan, L; Uversky, VN; Zaslavsky, BY
nationality International
journal BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
author keywords Protein structure; Protein partition; Aqueous two-phase system; Protein flexibility
keywords SOLVATION ENERGY RELATIONSHIP; SOLVENT PROPERTIES; METHYLENE GROUP; HYDROPHOBICITY; FLEXIBILITY; PREDICTION; COEFFICIENTS; RECOGNITION; CHARACTER; DYNAMICS
abstract Partitioning of 15 proteins in dextran-70-polyethylene glycol (PEG)-8000 aqueous two-phase systems (ATPSs) in the presence of 0.01 M sodium phosphate buffer, pH 7.4 was studied. The effect of salt additives (NaCl, CsCl, Na2SO4, NaClO4 and NaSCN) at different concentrations on the protein partition behavior was examined. The salt effects on protein partitioning were analyzed by using the Collander solvent regression relationship between the protein partition coefficients in ATPSs with and without salt additives. The results obtained show that the presence and concentration of salt additives affect the protein partition behavior. Analysis of ATPSs in terms of the differences between the relative hydrophobicity and electrostatic properties of the phases does not explain the protein partition behavior. The differences between protein partitioning could not be explained by the protein size. The structural signatures for the proteins were constructed from partition coefficient values in four ATPSs with different salt additives, and the structural distances were calculated using cytochrome c as the reference structure. The structural distances for all the examined proteins (except lysozyme) were found to be interrelated. Analysis of about 50 different descriptors of the protein structures revealed that the partition behavior of proteins is determined by the peculiarities of their surfaces (e.g., the number of water-filled cavities and the averaged hydrophobicity of the surface residues) and by the intrinsic flexibility of the protein structure measured in terms of the B-factor (or temperature factor). (c) 2014 Elsevier B.V. All rights reserved.
publisher ELSEVIER SCIENCE BV
issn 1570-9639
year published 2014
volume 1844
issue 3
beginning page 694
ending page 704
digital object identifier (doi) 10.1016/j.bbapap.2014.01.016
web of science category Biochemistry & Molecular Biology; Biophysics
subject category Biochemistry & Molecular Biology; Biophysics
unique article identifier WOS:000333491100024
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journal impact factor 2.371
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