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Updated: Aug 4, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
[Change in conformation of proteins in aqueous solutions of heterofunctional nonelectrolytes]
A P Zhukovskiĭ1, N V Rovnov, S V Sorvin
1Physical Department St. Petersburg State University, Russia.
Abstract:
In narrow ranges of concentrations of heterofunctional nonelectrolytes in aqueous solutions, structural transitions occur, which manifest themselves in the self-association of nonelectrolytes molecules and are accompanied by the screening of their hydrophobic groups from the contact with the solvent. In the same nonelectrolytes concentration ranges, conformational changes of protein molecules in solutions take place. The compatibility of the concentration ranges of these two processes is due to the fact that when nonelectrolytes molecules are extruded from the network of hydrogen bonds during the structural transition, both the self-association of nonelectrolytes molecules and their incorporation into the hydrate shell of the protein occur. The dehydration of the protein results in the disturbance of the balance of intra- and intermolecular interactions maintaining the native protein structure, which leads to the rearrangement of the macromolecule conformation.
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