Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface

Journal of Molecular Biology

Volumn 303, Issue 4, 2000, Pages 555-565

  Liu, Kai ^a   Cho, Ho S ^a   Hoyt, David W ^b   Nguyen, Tuan N ^a   Olds, Peter ^a   Kelly, Jeffery W ^c   Wemmer, David E ^a  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Amyloid; Hydrogen exchange; NMR spectroscopy; Protection factor; Transthyretin

Indexed keywords

AMYLOID; DEUTERIUM; PREALBUMIN; PROTEIN SUBUNIT; PROTON;

AMINO ACID SUBSTITUTION; ARTICLE; ESCHERICHIA COLI; HYDROGEN BOND; IN VIVO STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; STRUCTURE ANALYSIS;

EID: 0034602241     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4164     Document Type: Article

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