Experimental and theoretical evaluation of multisite cadmium(II) exchange in designed three-stranded coiled-coil peptides

Journal of the American Chemical Society

Volumn 134, Issue 14, 2012, Pages 6191-6203

  Chakraborty, Saumen ^a,d   Iranzo, Olga ^a,c   Zuiderweg, Erik R P ^b   Pecoraro, Vincent L ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^d UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MODELS; BIOLOGICAL MACROMOLECULE; CHEMICAL EXCHANGE; COILED COIL; EXCHANGE KINETICS; EXPERIMENTAL DATA; HELICAL BUNDLE; HELICAL STRUCTURES; HIGH AFFINITY; INTERACTIONS WITH SURFACES; ION PAIRS; LINE BROADENING; METAL BINDING SITES; METAL COMPLEXATION; METAL COMPLEXING; MOLECULAR REARRANGEMENT; MULTI-SITE; NATIVE SYSTEM; NMR SIGNALS; NUMERICAL INTEGRATIONS; PRIMARY BINDING SITES; SALT BRIDGES; THEORETICAL EVALUATION; THIOLATES; TIME REGIME;

AMINO ACIDS; BINDING SITES; CADMIUM COMPOUNDS; CHEMICAL SHIFT; COMPUTER SIMULATION; DIFFERENTIAL EQUATIONS; ION EXCHANGE; MATHEMATICAL MODELS; MERCURY COMPOUNDS; METAL IONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUMERICAL METHODS; PEPTIDES;

CADMIUM;

CADMIUM; CADMIUM BINDING PROTEIN; GLUTAMIC ACID; GLUTAMINE; LYSINE; METAL ION;

ARTICLE; BINDING KINETICS; BINDING SITE; CHEMICAL INTERACTION; COMPLEX FORMATION; ION EXCHANGE; METAL BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PH; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; TERMINAL SEQUENCE;

AMINO ACID SEQUENCE; ANISOTROPY; BINDING SITES; CADMIUM; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; METALS; MODELS, CHEMICAL; MODELS, THEORETICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, ULTRAVIOLET; X-RAYS;

EID: 84859608003     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja210510g     Document Type: Article

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