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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-22 2:00 |
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Conference: Bucharest University Faculty of Physics 2012 Meeting
Section: Solid State Physics and Materials Science
Title:
Binding interactions between Ni2+ ion and bovine serum albumin
Authors:
Ana IOANID, Marilena DIEACONU, Sorina IFTIMIE, S. ANTOHE
Affiliation:
Electricity, Solid State and Biophysics Department, Faculty of Physics, University of Bucharest
E-mail
sorina.iftimie@fizica.unibuc.ro
Keywords:
bovine serum albumin, Gibbs free energy, UV-absorbance
Abstract:
We present the results of an analysis of the near UV-spectra of the Ni-BSA system in solution, with the stoichiometry [1:1]M . UV-absorbance spectroscopy is adequate because the binding/dissociation ligand-protein processes are slow on the spectroscopic time scale. The difference UV-absorbance spectrum of this system shows a marked dependence both on the analytical ion concentration in solution and the time at macroscopic scale. The equilibrium constant of the binding reaction and the rate constant of the slow hysteresis effects were determined and at last the Gibbs free energy of the binding process were evaluated. The analysis of the results takes into account that the binding energy that measure the affinity of the partners, has two additive contributions, namely enthalping binding that comes via specific (polar) molecular interactions, such as hydrogen bonds, disulfide bonds, electrostatic, van der Waals, and entropic binding that results from nonspecific (apolar) hydrophobic interactions.Knowledge of the binding mechanisms is very important because the binding/dissociation kinetics of the ligand-protein determines ultimately the time scale to preserve a functioning conformational state of protein.
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