Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Intramural Research (Z01)
Project #
1Z01DK024150-25
Application #
2711551
Study Section
Large Bowel and Pancreatic Cancer Review Committee (LBP)
Project Start
Project End
Budget Start
Budget End
Support Year
25
Fiscal Year
1996
Total Cost
Indirect Cost
City
State
Country
United States
Zip Code
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

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