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Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes

✍ Scribed by R. A. Curtis; A. Montaser; J. M. Prausnitz; H. W. Blanch


Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
7 KB
Volume
58
Category
Article
ISSN
0006-3592

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Protein-protein and protein-salt interac
✍ R. A. Curtis; J. M. Prausnitz; H. W. Blanch πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 167 KB πŸ‘ 1 views

Protein-protein and protein-salt interactions have been obtained for ovalbumin in solutions of ammonium sulfate and for lysozyme in solutions of ammonium sulfate, sodium chloride, potassium isothiocyanate, and potassium chloride. The two-body interactions between ovalbumin molecules in concentrated

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The free energy difference between folded and unfolded state is about the same for most proteins and it is not more than the energy of a few noncovalent interactions. In addition to the numerous noncovalent interactions, some proteins contain one or more disulfide bonds, which, as covalent crosslink

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The determination of free energies that govern protein-protein recognition is essential for a detailed molecular understanding of biological specificity. Continuum models of macromolecular interactions, in which the solvent is treated by an implicit representation and the proteins are treated semi-m

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Measurements performed on biological systems, such as parts of plants, seeds and animals reveal non-exponential decay of the spin-spin relaxation function. Such behaviour has also been observed in the eye lens, which is a relative simple system mainly built from water, 65% of total weight, and 35% o

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During recombinant E. coli fermentation with high-expression levels inclusion bodies are often formed. Aqueous two-phase systems have been successfully used in the presence of urea for the initial recovery step of inclusion bodies from E. coli. Basic studies of the complex interactions are lacking.