Thermodynamic study of Cu 2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

Journal of Biological Inorganic Chemistry

Volumn 17, Issue 1, 2012, Pages 37-47

  Trapaidze, Ana ^a,b,c   Hureau, Christelle ^a,b   Bal, Wojciech ^d   Winterhalter, Mathias ^c   Faller, Peter ^a,b  

^a CNRS   (France)

^b UNIVERSITÉ DE TOULOUSE   (France)

^c JACOBS UNIVERSITY BREMEN   (Germany)

^d INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

Author keywords

Albumin; Bioinorganic chemistry Copper; Calorimetry; Peptide; Thermodynamics

Indexed keywords

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; AMYLOID BETA PROTEIN; ASPARAGINYLALANYLHISTIDYLLYSINE; BUFFER; COPPER; GLYCINE; GLYCYCLHISTIDYLLYSINE; PEPTIDE; UNCLASSIFIED DRUG; ASPARTYL ALANYL HISTIDYL LYSINE; ASPARTYL-ALANYL-HISTIDYL-LYSINE; CHELATING AGENT; GLYCYL HISTIDYL LYSINE; GLYCYL-HISTIDYL-LYSINE; LIGAND; OLIGOPEPTIDE;

ABSORPTION SPECTROPHOTOMETRY; ARTICLE; BINDING SITE; CHEMICAL REACTION; CHEMICAL STRUCTURE; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENTHALPY; HUMAN; IONIZATION; ISOTHERMAL TITRATION CALORIMETRY; METAL BINDING; PH; POTENTIOMETRY; PRIORITY JOURNAL; PROTON TRANSPORT; STOICHIOMETRY; THERMODYNAMICS; CALORIMETRY; CHEMISTRY;

BINDING SITES; CALORIMETRY; CHELATING AGENTS; COPPER; GLYCINE; LIGANDS; MOLECULAR STRUCTURE; OLIGOPEPTIDES; THERMODYNAMICS;

EID: 84857521038     PISSN: 09498257     EISSN: 14321327     Source Type: Journal    
DOI: 10.1007/s00775-011-0824-5     Document Type: Article

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