The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small-Angle X-Ray Scattering Study
- 1 January 2010
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 98 (1) , 147-157
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solutionJournal of The Royal Society Interface, 2009
- Absence of equilibrium cluster phase in concentrated lysozyme solutionsProceedings of the National Academy of Sciences, 2008
- Protein Interactions Studied by SAXS: Effect of Ionic Strength and Protein Concentration for BSA in Aqueous SolutionsThe Journal of Physical Chemistry B, 2006
- Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle X-ray scattering, fluorescence and circular dichroismBrazilian Journal of Physics, 2004
- The Atomic Structure of Human Methemalbumin at 1.9 ÅBiochemical and Biophysical Research Communications, 2002
- Scattering Functions of Semiflexible Polymers with and without Excluded Volume EffectsMacromolecules, 1996
- SANS studies of concentrated protein solutions. I. Bovine serum albuminBiopolymers, 1986
- Analysis of non-ideal behavior in concentrated hemoglobin solutionsJournal of Molecular Biology, 1977
- Electrophoretic Behavior of Bovine Plasma Albumin At Low pHJournal of the American Chemical Society, 1957
- Röntgenuntersuchung gelöster FadenmoleküleRecueil des Travaux Chimiques des Pays-Bas, 1949