title: Protein crystal nucleation: is the pair interaction potential the primary determinant of kinetics?
abstract: Fundamental understanding of protein crystal nucleation facilitates crystallization of biological macromolecules for structure determination and control of crystal size distribution. In the studies presented here, nucleation kinetics of hen egg-white lysozyme crystals were measured at solution conditions that exhibited equal solubility by adjusting pH, temperature, or sodium chloride concentration. It was observed that solution conditions that lead to equal solubility resulted in equal nucleation rates and hence kinetic parameters. Since the solubility of globular proteins correlates with the osmotic second virial coefficient, B(22), an integral measure of the protein pair interaction potential, this observation indicates that the protein pair interaction plays a key role in determining nucleation kinetic parameters.
authors.affiliation: Department of Chemical & Environmental Engineering, University of Toledo, 2801 W. Bancroft St., Toledo, OH 43606, USA.
authors.forename: Venkateswarlu
authors.initials: V
authors.lastname: Bhamidi
authors.forename: Sasidhar
authors.initials: S
authors.lastname: Varanasi
authors.forename: Constance A
authors.initials: CA
authors.lastname: Schall
mesh_terms: D000818:Animals; D002645:Chickens; D003460:Crystallization; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D013696:Temperature
chemical_list: D011506:Proteins; D009113:Muramidase