Determining Thermodynamic Parameters from Isothermal Calorimetric Isotherms of the Binding of Macromolecules to Metal Cations Originally Chelated by a Weak Ligand

Autor:	Lanying Q. Hatcher, William D. Bush, Lian Hong, John D. Simon
Rok vydání:	2007
Předmět:	Chemistry Isothermal titration calorimetry Ligand (biochemistry) Binding constant Isothermal process Surfaces Coatings and Films Metal Crystallography visual_art Materials Chemistry visual_art.visual_art_medium Chelation Physical and Theoretical Chemistry Stoichiometry Macromolecule
Zdroj:	The Journal of Physical Chemistry B. 112:604-611
ISSN:	1520-5207 1520-6106
Popis:	An accurate data analysis method for determining stoichiometry and thermodynamic parameters from isothermal titration calorimetry data for the binding of macromolecules to metal cations that are solubilized through an association with a weak ligand is presented. This approach is applied to determine the binding constant for the association of Cu(II) to the first 16 residues of the Alzheimer's amyloid beta peptide, Abeta(1-16) under conditions where Cu(II) is rendered soluble through weak binding to glycine. At pH 7.2 and 37 degrees C, a binding constant of 1.5 x 10(9) M-1 (Kd = 0.7 nM) is determined for the association of Cu(II) with Abeta(1-16).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c93b83a3c08b0684c6cd97c5a6e7e571 https://doi.org/10.1021/jp075747r Zobrazit plný text záznamu