Calibrative approaches to protein solubility modeling of a mutant series using physicochemical descriptors.

ABSTRACT: A set of physicochemical properties describing a protein of known structure is employed for a calibrative approach to protein solubility. Common hydrodynamic and electrophoretic properties routinely measured in the bio-analytical laboratory such as zeta potential, dipole moment, the second osmotic virial coefficient are first estimated in silico as a function a pH and solution ionic strength starting with the protein crystal structure. The utility of these descriptors in understanding the solubility of a series of ribonuclease Sa mutants is investigated. A simple two parameter model was trained using solubility data of the wild type protein measured at a restricted number of solution pHs. Solubility estimates of the mutants demonstrate that zeta potential and dipole moment may be used to r

SUBMITTER: Long WF 

PROVIDER: S-EPMC2956060 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature