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Protein solubility modelingA 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. Copyright 1999 John Wiley & Sons, Inc.
Document ID
20040147352
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Agena, S. M.
(NASA Marshall Space Flight Center Huntsville AL United States)
Pusey, M. L.
Bogle, I. D.
Date Acquired
August 22, 2013
Publication Date
July 20, 1999
Publication Information
Publication: Biotechnology and bioengineering
Volume: 64
Issue: 2
ISSN: 0006-3592
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other

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