Noncovalent Intermolecular Interactions in Biochemistry

Minton, A P.

Abstract

A novel experimental method for rapid qualitative characterization of heterogeneous mixtures of macrosolutes has been proposed, based upon analysis of the time and concentration dependence of two experimentally measurable parameters called the apparent sedimentation and diffusion coefficients. A simple method for reducing the duration of a conventional sedimentation equilibrium by a factor of approximately five has been proposed. The interaction between fibrous rabbit muscle actin and several globular proteins has been investigated via size exclusion chromatography, sedimentation, and viscosity measurement. A PC-based data acquisition and control system for the UV-visible scanner on the Beckman Model E analytical centrifuge has been developed and installed. An approximate theory has been formulated for the dependence of the diffusion coefficient of each species of protein upon the concentrations of all species in a mixture of globular proteins.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
• Type: Intramural Research (Z01)
• Project #: 1Z01DK024150-18
• Application #: 3917570
• Support Year: 18
• Fiscal Year: 1988

Institution

• Name: U.S. National Inst Diabetes/Digst/Kidney
• Country: United States

Publications

Minton, Allen P (2006) Macromolecular crowding. Curr Biol 16:R269-71

Howlett, Geoffrey J; Minton, Allen P; Rivas, German (2006) Analytical ultracentrifugation for the study of protein association and assembly. Curr Opin Chem Biol 10:430-6

Minton, Allen P (2006) How can biochemical reactions within cells differ from those in test tubes? J Cell Sci 119:2863-9

Kameyama, Keiichi; Minton, Allen P (2006) Rapid quantitative characterization of protein interactions by composition gradient static light scattering. Biophys J 90:2164-9

Ellis, R John; Minton, Allen P (2006) Protein aggregation in crowded environments. Biol Chem 387:485-97

McPhie, Peter; Ni, Yi-sheng; Minton, Allen P (2006) Macromolecular crowding stabilizes the molten globule form of apomyoglobin with respect to both cold and heat unfolding. J Mol Biol 361:7-10

Attri, Arun K; Minton, Allen P (2005) Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solution. Anal Biochem 346:132-8

Attri, Arun K; Minton, Allen P (2005) New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. Anal Biochem 337:103-10

Minton, Allen P (2005) Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J Pharm Sci 94:1668-75

Hall, Damien; Minton, Allen P (2005) Turbidity as a probe of tubulin polymerization kinetics: a theoretical and experimental re-examination. Anal Biochem 345:198-213