Protein solubility modeling.

Abstract:

:A thermodynamic framework (UNIQUAC model with temperature dependent parameters) is applied to model the salt-induced protein crystallization equilibrium, i.e., protein solubility. The framework introduces a term for the solubility product describing protein transfer between the liquid and solid phase and a term for the solution behavior describing deviation from ideal solution. Protein solubility is modeled as a function of salt concentration and temperature for a four-component system consisting of a protein, pseudo solvent (water and buffer), cation, and anion (salt). Two different systems, lysozyme with sodium chloride and concanavalin A with ammonium sulfate, are investigated. Comparison of the modeled and experimental protein solubility data results in an average root mean square deviation of 5.8%, demonstrating that the model closely follows the experimental behavior. Model calculations and model parameters are reviewed to examine the model and protein crystallization process.

journal_name

Biotechnol Bioeng

authors

Agena SM,Pusey ML,Bogle ID

doi

10.1002/(sici)1097-0290(19990720)64:2<144::aid-bit

subject

Has Abstract

pub_date

1999-07-20 00:00:00

pages

144-50

issue

2

eissn

0006-3592

issn

1097-0290

pii

10.1002/(SICI)1097-0290(19990720)64:2<144::AID-BIT

journal_volume

64

pub_type

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