title: The thermodynamics of protein interactions with essential first row transition metals.
abstract: BACKGROUND
  The binding of metal ions to proteins is a crucial process required for their catalytic activity, structural stability and/or functional regulation. Isothermal titration calorimetry provides a wealth of fundamental information which when combined with structural data allow for a much deeper understanding of the underlying molecular mechanism.
  
  
  METHODS
  A rigorous understanding of any molecular interaction requires in part an in-depth quantification of its thermodynamic properties. Here, we provide an overview of recent studies that have used ITC to quantify the interaction of essential first row transition metals with relevant proteins and highlight major findings from these thermodynamic studies.
  
  
  CONCLUSIONS
  The thermodynamic characterization of metal ion-protein interactions is one important step to understanding the role that metal ions play in living systems. Such characterization has important implications not only to elucidating proteins' structure-function relationships and biological properties but also in the biotechnology sector, medicine and drug design particularly since a number of metal ions are involved in several neurodegenerative diseases.
  
  
  CONCLUSIONS
  Isothermal titration calorimetry measurements can provide complete thermodynamic profiles of any molecular interaction through the simultaneous determination of the reaction binding stoichiometry, binding affinity as well as the enthalpic and entropic contributions to the free energy change thus enabling a more in-depth understanding of the nature of these interactions.
authors.affiliation: State University of New York at Potsdam, Potsdam, NY 13676, United States. Electronic address: bouabdf@potsdam.edu.
authors.forename: Fadi
authors.initials: F
authors.lastname: Bou-Abdallah
authors.affiliation: State University of New York at Potsdam, Potsdam, NY 13676, United States.
authors.forename: Thomas R
authors.initials: TR
authors.lastname: Giffune
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D002256:Carbonic Anhydrases / Q000737:chemistry*; D027682:Cation Transport Proteins / Q000737:chemistry*; D002417:Cattle; D000079922:Copper Transport Proteins; D000073840:Copper-Transporting ATPases; D005293:Ferritins / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D056511:Metallochaperones / Q000737:chemistry*; D008670:Metals / Q000737:chemistry*; D018832:Molecular Chaperones; D011485:Protein Binding; D013482:Superoxide Dismutase / Q000737:chemistry*; D000072105:Superoxide Dismutase-1; D013816:Thermodynamics; D014168:Transferrin / Q000737:chemistry; D028561:Transition Elements / Q000737:chemistry*
chemical_list: C474500:ATOX1 protein, human; D027682:Cation Transport Proteins; D000079922:Copper Transport Proteins; D056511:Metallochaperones; D008670:Metals; D018832:Molecular Chaperones; C000606290:SOD1 protein, human; D014168:Transferrin; D028561:Transition Elements; D005293:Ferritins; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1; D000251:Adenosine Triphosphatases; D002256:Carbonic Anhydrases; D000073840:Copper-Transporting ATPases
keywords: Binding; Enthalpy/entropy; Isothermal titration calorimetry (ITC); Proteins; Thermodynamics; Transitions metal ions