The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques

Journal of Molecular Biology

Volumn 422, Issue 3, 2012, Pages 390-402

  Yanagi, Kotaro ^a   Sakurai, Kazumasa ^a   Yoshimura, Yuichi ^a   Konuma, Tsuyoshi ^b   Lee, Young Ho ^a   Sugase, Kenji ^b   Ikegami, Takahisa ^a   Naiki, Hironobu ^c   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b SUNTORY INSTITUTE FOR BIOORGANIC RESEARCH   (Japan)

^c UNIVERSITY OF FUKUI   (Japan)

Author keywords

amyloid fibril; NMR; transferred cross saturation; transient complex

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; MONOMER;

ANIMAL CELL; ARTICLE; CHEMICAL INTERACTION; CHEMICAL STRUCTURE; DNA DENATURATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN UNFOLDING; RELAXATION TIME;

EID: 84865098615     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.05.034     Document Type: Article

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