Increase in the conformational flexibility of β 2-microglobulin upon copper binding: A possible role for copper in dialysis-related amyloidosis

Protein Science

Volumn 13, Issue 3, 2004, Pages 797-809

  Villanueva, James ^a,d   Hoshino, Masaru ^a   Katou, Hidenori ^a   Kardos, József ^a   Hasegawa, Kazuhiro ^b   Naiki, Hironobu ^b,c   Goto, Yuji ^a,c  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF FUKUI   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d University of the Philippines Diliman   (Philippines)

Author keywords

2 microglobulin; Amyloid fibrils; Copper binding; Dialysis related amyloidosis; Heteronuclear NMR; Hydrogen deuterium exchange; Protein folding misfolding

Indexed keywords

AMIDE; AMYLOID PRECURSOR PROTEIN; BETA 2 MICROGLOBULIN; COPPER; DEUTERIUM; HISTIDINE; HYDROGEN; SERINE; VALINE;

AMYLOIDOSIS; ARTICLE; DIALYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY;

ALGORITHMS; AMIDES; AMYLOIDOSIS; BETA 2-MICROGLOBULIN; BINDING SITES; CIRCULAR DICHROISM; COPPER; DEUTERIUM EXCHANGE MEASUREMENT; HEAT; HISTIDINE; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PLIABILITY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; RENAL DIALYSIS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 1342289275     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03445704     Document Type: Article

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