Bovine serum albumin conformation

Curvale, R. Masuelli, M. Perez Padilla, A. 2008. Intrinsic viscosity of bovine serum albumin conformers. International Journal of Biological Macromolecules 42, 133-137. 

Mir MM, Fazili KM, Abul Qasim M. Chemical modification of buried lysine residues of bovine serum albumin and its influence on protein conformation and bilirubin binding. Biochim. Biophys. Acta 1992 1119 261-267. 

J.R. Lu, T.J. Su, and R.K. Thomas Structural Conformation of Bovine Serum Albumin Layers at the Air-Water Interface Studied by Neutron Reflection. I. Colloid Interface Sci. 213, 426 (1999). 

Reed, R. G., Feldhoff, R. C., Clute, O. L. and Peters, T., Jr. 1975. Fragments of bovine serum albumin produced by limited proteolysis. Conformation and ligand bonding. Biochemistry 14, 4578-4583. 

Taylor, R. P Berga, S., Chau, V. and Bryner, C. 1975A. Bovine serum albumin as a catalyst. III. Conformational studies. J. Am. Chem. Soc. 97, 1943-1948. 

White, D. D., Stewart, S. and Wood, G. C. 1973. The use of reporter group circular dichroism in the study of conformational transitions in bovine serum albumin. FEBS Lett. 33, 305-310. 

Absorbance of peptide bonds at 2170 nm is usually used as a key band for the calibration of protein content measurement. However, the intensity of the absorption depends on the structure and conformation of the protein. Yamashita et al [8] investigated the change in absorption at 2170 nm caused by the conformational change of protein using bovine serum albumin (BSA) as the model protein. A mixture of dithiothreitol (a reducing agent) and BSA (5%) was taken in a quartz cell attached to the NIR instrument, and then spectra were recorded at 10-minute intervals. Dithiothreitol reduced the disulfide bond in BSA. The... 

Servagent-Noinville, S., Revault, M., Quiquampoix, H., and Baron, M.-H. (2000). Conformational changes of bovine serum albumin induced by adsorption on different clay surfaces FTIR analysis. J. Coll. Interface Sci. 221,273-283. 

T13. Timmins, G. S., and Davies, M. J., Conformational changes induced in bovine serum albumin by the photodynamic action of haematoporphyrin. J. Photochem. Photobiol. B 24, 117-122 (1994). 

Effect of Ethanol on Conformational state of protein. To understand the effect of ethanol and pH in flavour-protein interactions the binding of y-decalactone to bovine serum albumin was investigated using the equilibrium dialysis method (20). Without ethanol, a decrease in pH (from 5.3 to3.5) reduces by one-half the y-decalactone binding onto protein. In the presence of ethanol, changing pH do not have any appreciable effect (Table VI). 

---