determines entropy and sensitive to systematic entalpy errors limited to simple interaction models fluorescence very sensitive, suitable only for very 10-5 - 10-7 M spectroscopy consumes little material simple complex can follow native stoichiometries delivers apparent biomolecule or added competitor stability constants Table 2 Competitivity index (CI)a values for Gly binding of Cu(II) at pH 7.4b. Gly:Cu(II) cCu(II) = 104 M cCu(II) = 103 M 1 6.03 6.00 2 7.11 7.98 4 7.96 8.92 a computational entity, defined as the logarithm of the conditional stability constant of MZ (the metal complex of a theoretical molecule Z), such that = [MZ] [41, 42]. Σijkl([MiHjLkAl] b The binding constants from ref. [40] were used for calculations. Table 3. Literature values for the stability constants of Cu2+ complexes with (aS) and its α-synuclein mutants. WT denotes wild-type aS. Only the strong binding site is described. aS cKML T protein pH conc. Method Buffer ref. (°C) (μM)
determines entropy and entalpy sensitive to systematic errors limited to simple interaction models fluorescence spectroscopy very sensitive, consumes little material can follow native biomolecule or added competitor suitable only for very simple complex stoichiometries delivers apparent stability constants 10-5 - 10-7 M Table 2 Competitivity index (CI)a values for Gly binding of Cu(II) at pH 7.4b. Gly:Cu(II) cCu(II) = 104 M cCu(II) = 103 M 1 6.03 6.00 2 7.11 7.98 4 7.96 8.92 a computational entity, defined as the logarithm of the conditional stability constant of MZ (the metal complex of a theoretical molecule Z), such that Σijkl([MiHjLkAl] = [MZ] [41, 42]. b The binding constants from ref. [40] were used for calculations. Table 3. Literature values for the stability constants of Cu2+ complexes with α-synuclein (aS) and its mutants. WT denotes wild-type aS. Only the strong binding site is described. protein cKML pH T (°C) aS conc. (μM) Method Buffer ref.
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