Noncovalent Intermolecular Interactions in Biochemistry

Minton, A P.

Abstract

The interaction between fibrous rabbit muscle actin and four globular proteins in solutions of physiological ionic strength has been studied by means of sedimentation equilibrium and viscosity. Techniques for optimization of experimental protocols and data analysis in the quantitative characterization of macromolecular hetero-associations via measurement of sedimentation equilibrium have been carried out via simulation studies. The effect of high protein concentration upon the sedimentation coefficient of serum albumin has been carefully measured as a function of pH and ionic strength. Fully automated scanner control capability has been added to a custom-designed and built PC-based data acquisition system for the Beckman Model E analytical ultracentrifuge.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
• Type: Intramural Research (Z01)
• Project #: 1Z01DK024150-19
• Application #: 3875723
• Support Year: 19
• Fiscal Year: 1990

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

Gonzalez, Jose Manuel; Velez, Marisela; Jimenez, Mercedes et al. (2005) Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils. Proc Natl Acad Sci U S A 102:1895-900

Minton, Allen P (2005) Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisited. Biophys J 88:971-85

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