Analyzing the Size of Albumin Macromolecules in Aqueous Solutions

Changes in the structure and size of macromolecules of human and bovine serum albumin in aqueous solutions are considered, depending on temperature, concentration, and acid–base equilibrium. It is found that a change in the hydrodynamic radius of the macromolecule is an indicator of the structural p...

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Bibliographic Details
Published in:Russian Journal of Physical Chemistry A 2021-02, Vol.95 (2), p.303-309
Main Authors: Malomuzh, N. P., Khorolskyi, A. V.
Format: Article
Language:English
Subjects:
Aqueous solutions
Chemical bonds
Chemistry
Chemistry and Materials Science
Macromolecules
Phase transitions
Physical Chemistry
Physical Chemistry of Solutions
Proteins
Self diffusion
Serum albumin
Shear viscosity
Water chemistry
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Summary:Changes in the structure and size of macromolecules of human and bovine serum albumin in aqueous solutions are considered, depending on temperature, concentration, and acid–base equilibrium. It is found that a change in the hydrodynamic radius of the macromolecule is an indicator of the structural phase transformations of globular proteins. Ways of determining the radii of macromolecules from data on the shear viscosity of solutions and the self-diffusion of macromolecules in them are discussed. The hydrodynamic radii of albumin macromolecules found by these means are compared. It is shown that conclusions can be drawn about the nature of bonding between water molecules and protein macromolecules using the obtained data.
ISSN:0036-0244
1531-863X
DOI:10.1134/S0036024421020199