The role of disulfide bond in the amyloidogenic state of β2-microglobulin studied by heteronuclear NMR

Protein Science

Volumn 11, Issue 9, 2002, Pages 2218-2229

  Katou, Hidenori ^a   Kanno, Takashi ^a   Hoshino, Masaru ^a   Hagihara, Yoshihisa ^a   Tanaka, Hiroyuki ^a   Kawai, Tomoji ^a   Hasegawa, Kazuhiro ^b   Naiki, Hironobu ^b   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF FUKUI   (Japan)

Author keywords

2 microglobulin; Amyloid fibrils; Atomic force microscopy; Denatured state; Disulfide bond; Heteronuclear NMR; Hydrogen deuterium exchange

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; CYSTEINE; DISULFIDE; HYDROGEN; NITROGEN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; BETA SHEET; CONFORMATIONAL TRANSITION; DISULFIDE BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; CHEMISTRY; GENETICS; HUMAN; HYDROGEN BOND; METABOLISM; OXIDATION REDUCTION REACTION; PH; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; BETA 2-MICROGLOBULIN; DISULFIDES; HUMAN; HYDROGEN; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ATOMIC FORCE; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SUPPORT, NON-U.S. GOV'T; HUMANS;

EID: 0036708005     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0213202     Document Type: Article

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