Solvent interaction analysis of intrinsically disordered proteins in aqueous two-phase systems
authors Breydo, L; Mikheeva, LM; Madeira, PP; Zaslavsky, BY; Uversky, VN
nationality International
journal MOLECULAR BIOSYSTEMS
keywords NATIVELY UNFOLDED PROTEINS; ANTI-SIGMA FACTOR; C-TERMINAL HALF; UNSTRUCTURED PROTEINS; ALPHA-SYNUCLEIN; FUNCTIONAL ANTHOLOGY; STRUCTURAL DISORDER; MOLECULAR CONFINEMENT; PARKINSONS-DISEASE; COEXISTING PHASES
abstract In an aqueous two-phase system (ATPS), the partitioning of a protein is defined by the differential interactions of the protein with aqueous media in the two phases. Our study shows that partitioning of proteins in a set of ATPSs of different ionic compositions can be used to quantify structural differences between a-synuclein, its variants and several globular proteins. Since application of ATPSs implies the use of high concentrations of two polymers in water when a certain threshold concentration of the polymers is exceeded, and since these levels of polymer concentrations are similar to those commonly used to mimic the effects of macromolecular crowding on proteins, we used circular dichroism spectroscopy to evaluate the structural consequences of placing proteins in solutions with high polymer concentrations and various ionic compositions.
publisher ROYAL SOC CHEMISTRY
issn 1742-206X
year published 2013
volume 9
issue 12
beginning page 3068
ending page 3079
digital object identifier (doi) 10.1039/c3mb70329k
web of science category Biochemistry & Molecular Biology
subject category Biochemistry & Molecular Biology
unique article identifier WOS:000326461000014
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journal impact factor 3.336
5 year journal impact factor 2.986
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