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Updated: May 6, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Concentration-dependent viscosity of binary and ternary mixtures of nonassociating proteins: measurement and analysis
1Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services , Building 8, Room 226, Bethesda, Maryland 20892-0830, United States.
Abstract:
Using a recently developed automated viscometer (Grupi, A.; Minton, A. P. Anal. Chem. 2012, 84, 10732-10736), the dependence of solution viscosity upon the concentrations of bovine serum albumin, hen egg ovomucoid, and human fibrinogen have been measured individually and in binary and ternary mixtures over a wide range of compositions and at total concentrations of up to 300 g/L. The concentration dependence of viscosity of all solutions is quantitatively described over the entire range of concentrations and compositions by a semiempirical equation requiring specification of only two composition-independent global parameters per protein.
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