Protein solubility modeling

✍ Scribed by Sabine M. Agena; Marc L. Pusey; I. David L. Bogle

• Book ID: 101242343
• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 88 KB
• Volume: 64
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(19990720)64:2<144::aid-bit3>3.0.co;2-p

✦ Synopsis

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.