B.S., University of California, Los Angeles, 1964
Ph.D., University of California, Los Angeles, 1968
Research Statement
This laboratory is engaged in theoretical and experimental studies of noncovalent interactions -- both attractive and repulsive -- between like and unlike biological macromolecules in solution and on surfaces. Novel experimental methods for the quantitative characterization of such interactions in solution, based upon the measurement and analysis of sedimentation equilibrium and light scattering, have been developed and are being developed. The effect of excluded volume ("macromolecular crowding") and surface interactions on the equilibria and kinetics of a variety of model reactions are studied experimentally and theoretically.
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Selected Publications
1. Jimenez M, Rivas G, Minton AP Quantitative Characterization of Weak Self-Association in Concentrated Solutions of Immunoglobulin G via the Measurement of Sedimentation Equilibrium and Osmotic Pressure. Biochemistry(46): 8373-8378, 2007. [Full Text/Abstract]
2. Minton AP Static light scattering from concentrated protein solutions, I: general theory for protein mixtures and application to self-associating proteins. Biophys J(93): 1321-8, 2007. [Full Text/Abstract]
3. Minton AP The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins. J Pharm Sci, 2007. [Full Text/Abstract]
4. Minton AP How can biochemical reactions within cells differ from those in test tubes? J Cell Sci(119): 2863-9, 2006. [Full Text/Abstract]
5. Kameyama K, Minton AP Rapid quantitative characterization of protein interactions by composition gradient static light scattering. Biophys J(90): 2164-9, 2006. [Full Text/Abstract]
6. Minton AP Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J Pharm Sci(94): 1668-75, 2005. [Full Text/Abstract]
7. Minton AP Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisited. Biophys J (88): 971-85, 2005. [Full Text/Abstract]
8. Attri AK, Minton AP 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, 2005. [Full Text/Abstract]
9. Zorrilla S Jimenez M Lillo P Rivas G Minton AP Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease. Biophys Chem (108): 89-100, 2004. [Full Text/Abstract]
10. Sasahara K McPhie P Minton AP Effect of dextran on protein stability and conformation attributed to macromolecular crowding. J Mol Biol (326): 1227-37, 2003. [Full Text/Abstract]
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