Determination of the second virial coefficient of bovine serum albumin under varying pH and ionic strength by composition-gradient multi-angle static light scattering
| Autor: | Diana M. Acosta, Nicole F. Steinmetz, Roger H. French, Yingfang Ma, V. Adrian Parsegian, Jon Whitney, Rudolf Podgornik |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Light
Static Electricity Biophysics Analytical chemistry Sodium Chloride symbols.namesake Animals Scattering Radiation Static light scattering Bovine serum albumin Molecular Biology Original Paper Aqueous solution biology Chemistry Osmolar Concentration Intermolecular force Serum Albumin Bovine Cell Biology Atomic and Molecular Physics and Optics Isoelectric point Virial coefficient Ionic strength Hydrodynamics symbols biology.protein Cattle van der Waals force Protein Binding |
| Zdroj: | Journal of Biological Physics. 41:85-97 |
| ISSN: | 1573-0689 0092-0606 |
| Popis: | Composition-gradient multi-angle static light scattering (CG-MALS) is an emerging technique for the determination of intermolecular interactions via the second virial coefficient B22. With CG-MALS, detailed studies of the second virial coefficient can be carried out more accurately and effectively than with traditional methods. In addition, automated mixing, delivery and measurement enable high speed, continuous, fluctuation-free sample delivery and accurate results. Using CG-MALS we measure the second virial coefficient of bovine serum albumin (BSA) in aqueous solutions at various values of pH and ionic strength of a univalent salt (NaCl). The systematic variation of the second virial coefficient as a function of pH and NaCl strength reveals the net charge change and the isoelectric point of BSA under different solution conditions. The magnitude of the second virial coefficient decreases to 1.13 x 10(-5) ml*mol/g(2) near the isoelectric point of pH 4.6 and 25 mM NaCl. These results illuminate the role of fundamental long-range electrostatic and van der Waals forces in protein-protein interactions, specifically their dependence on pH and ionic strength. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink