Chinese Journal of Chemistry · 2007 · 10 citations · 8 references
Natural SciencesBiochemistryChemistryBiophysical ChemistryPhysical ChemistrySpectroscopyBinding ThermodynamicsChemical BondingHydrogen Bonding In BiomoleculesIntermolecular ForcesLigand BindingBinding ConstantsConformational StabilityConformational TransitionsFree Energy ChangesIon Binding SitesPh Dependence Of StabilityPh-dependent Biomolecular InteractionsProtein Fluorescence
Abstract The interaction between mercuric ion and apoCopC in the absence or presence of cupric ion was investigated through difference UV spectra in Hepes buffer (10 mmol·L −1 ) at pH 7.4. The results suggest that mercuric ion can bind to C ‐ and N ‐terminal binding sites of apoCopC, and the conditional binding constants were calculated to be k N =(6.79±1.12)×10 6 mol −1 ·L and k C =(3.06±0.05)×10 5 mol −1 ·L. Using urea as a chemical agent, the conformational stabilities of apoCopC and Hg 2+ N ‐CopC‐Hg 2+ C were monitored by fluorescence spectrum in Hepes buffer (50 mmol·L −1 ) at pH 7.4. The free energy of stabilization is (14.69±0.85) and (16.66±0.55) kJ·mol −1 , respectively. Hg 2+ N ‐CopC‐Hg 2+ C is more stable than apoCopC.
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Fabio Arnesano, Lucia Banci, Ivano Bertini et al. · Structure · 2002 · 103 citations · Full text
C-Terminal Half of Human Centrin 2 Behaves like a Regulatory EF-Hand Domain
Elena Matei, Simona Miron, Y. Blouquit et al. · Biochemistry · 2003 · 65 citations