Association between hydrophobically modified polyanions and negatively charged bovine serum albumin
Article Abstract:
Research was conducted to examine the association between hydrophobically modified polyanions (HMPA) and negatively charged bovine serum albumin (BSA) using light scattering, equilibrium dialysis and viscometry. Pronounced increases of the scattering depending on the hydrophobicity of the synthetic polymer revealed the formation of complexes. Results support the proposed mechanism of thickening, upon addition of protein, observed previously in semidilute solutions of HMPA.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
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Interfacial water structure controls protein conformation
Article Abstract:
A phenomenological theory of salt-induced Hofmeister phenomena, which is based on a relation between protein solubility in salt solutions and protein-water interfacial tension, is described. The results have supported the ability of the new formalism to account for the diverse manifestations of salt effects on protein conformation dynamics, and stability and to resolve the puzzle of chaotropes stabilizing certain proteins conformation.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2007
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