Spectroscopic Investigations of Interactions of Heteropolyacids with a-Lactalbumin Complexes
FATEMEH F. BAMOHARRAM
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
JAMSHID CHAMANI
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
MAJID M. HERAVI
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
OMID RAJABI
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
MINA ROSHANI
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
NASRIN KARIMI
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
OMID M. HERAVI
Department of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, IranDepartment of Chemistry, Islamic Azad University, Mashhad Branch, Mashhad, Iran
Corresponding Author(s) : FATEMEH F. BAMOHARRAM
fbamoharram@mshdiau.ac.ir
Asian Journal of Chemistry,
Vol. 21 No. 5 (2009): Vol 21 Issue 5
The interaction between a-lactalbumin with heteropoly acids occurred. The best denaturation of a-lactalbumin with Preyssler heteropoly acid occured in comparison with heteropoly acids including Keggin and Dawson structures. Based on calculated thermodynamics parameteres, it is shown that during denaturation of protein, preyssler heteropoly acid has the highest ΔG(H2O), m value and lowest Cm at the shortest time compared with other polyoxometalates (POMs) with Keggin and Dawson structures. The electrostatic interaction of protein with various heteropoly acids is important on a molecular level for the interpretation and development of model compounds with selective affinity for particular proteins.
F. BAMOHARRAM, F., CHAMANI, J., M. HERAVI, M., RAJABI, O., ROSHANI, M., KARIMI, N., & M. HERAVI, O. (2010). Spectroscopic Investigations of Interactions of Heteropolyacids with a-Lactalbumin Complexes. Asian Journal of Chemistry, 21(5), 3385–3394. Retrieved from https://asianpubs.org/index.php/ajchem/article/view/17311
