Patterns of protein–protein interactions in salt solutions and implications for protein crystallization
✍ Scribed by André C. Dumetz; Ann M. Snellinger-O'Brien; Eric W. Kaler; Abraham M. Lenhoff
- Book ID
- 111753021
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2007
- Tongue
- English
- Weight
- 380 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0961-8368
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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
## Abstract Protein–protein interactions were measured for ovalbumin and for lysozyme in aqueous salt solutions. Protein–protein interactions are correlated with a proposed potential of mean force equal to the free energy to desolvate the protein surface that is made inaccessible to the solvent due
Increasing the solubility of protein stock solutions to above that in a standard chromatography buffer (50 mM Tris-HCl pH 7.5, 100 mM NaCl) led to an increase in the number of crystallization conditions for ten globular proteins subjected to two crystal screens: the Index and Precipitant/Precipitant