Journal
PHYSICAL REVIEW LETTERS
Volume 84, Issue 6, Pages 1339-1342Publisher
AMERICAN PHYSICAL SOC
DOI: 10.1103/PhysRevLett.84.1339
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- NHLBI NIH HHS [R01 HL58038] Funding Source: Medline
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We have studied molecular interactions in solutions of the protein apoferritin by static and dynamic light scattering. When plotted against the electrolyte concentration, the second osmotic virial coefficient exhibits a minimum. The ascending branch of this dependence is a manifestation of a surprisingly strong repulsion between the molecules at electrolyte concentrations about and above 0.2M, where electrostatic interactions are suppressed. We argue that the repulsion is due to the water structuring, enhanced by the accumulation of hydrophilic counterions around the apoferritin molecules, giving rise to so-called hydration forces.
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