Noncovalent Intermolecular Interactions in Biochemistry

Minton, A P.

Abstract

The calcium-linked hetero-association of human complement subcomponents C1r and C1s has been quantitatively characterized as a function of calcium concentration via the technique of tracer sedimentation equilibrium. The role of macromolecular crowding in the regulation of cellular volume has been further explored. A new technique for the detection of associations in mixtures of several protein components, called sedimentation equilibrium- quantitative polyacrylamide gel electrophoresis (SE-QPAGE), has been developed and tested on mixtures of up to four protein components. Theoretical models have been proposed for the (i) effect of confining proteins to small pores of different shapes, and (ii) and the effect of weak nonspecific attractive interactions between surfaces and proteins upon various conformational and association equilibria.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
• Type: Intramural Research (Z01)
• Project #: 1Z01DK024150-22
• Application #: 3776192
• Support Year: 22
• Fiscal Year: 1993

Institution

• Name: National Institute of Diabetes and Digestive and Kidney Diseases
• 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