Molecular thermodynamics for some applications in biotechnology
Affiliation:
Department of Chemical Engineering, University of California, 201 Gilman Hall, Berkeley, CA 94720-1462, USA;Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA;Department of Veterinary Pharmacology and Toxicology, College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, China;Department of Physical Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz, Iran;School of Chemical Engineering and Technology, State Key Laboratory of Chemical Engineering, Tianjin University, Tianjin 300072, PR China;Centro de Investigação em Química, Department of Chemistry and Biochemistry, Faculty of Science, University of Porto, Rua do Campo Alegre, 687, P-4169-007 Porto, Portugal;Department of Chemistry, Texas Christian University, Fort Worth, TX 76129, USA;Department of Physical Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz, Iran
Abstract:
As biotechnology sweeps the world, it is appropriate to remember that the great virtue of thermodynamics is its broad range of applicability. As a result, there is a growing literature describing how chemical thermodynamics can be used to inform processes for old and new biochemical products for industry and medicine. A particular application of molecular thermodynamics concerns separation of aqueous proteins by selective precipitation. For this purpose, we need phase diagrams; for constructing such diagrams, we need to understand not only the qualitative nature of phase equilibria of aqueous proteins but also the quantitative intermolecular forces between proteins in solution. Some examples are given to show how aqueous protein–protein forces can be calculated or measured to yield a potential of mean force and how that potential is then used along with a statistical thermodynamic model to establish liquid–liquid and liquid–crystal equilibria. Such equilibria are useful not only for separation processes but also for understanding diseases like Alzheimer’s, cataracts and sickle-cell anemia that appear to be caused by protein agglomeration.
