High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility

Biochemical Journal

Volumn 450, Issue 2, 2013, Pages 321-332

  Amin, Nader T ^a   Wallis, A Katrine ^a   Wells, Stephen A ^b   Rowe, Michelle L ^c   Williamson, Richard A ^c   Howard, Mark J ^c   Freedman, Robert B ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b UNIVERSITY OF WARWICK   (United Kingdom)

^c UNIVERSITY OF KENT   (United Kingdom)

Author keywords

Endoplasmic reticulum; Endoplasmic reticulum protein 277 kDa (ERp27); NMR; Protein disulfide isomerase (PDI); Protein dynamics; Thioredoxin fold

Indexed keywords

ERP27 PROTEIN; MEMBRANE PROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTALLIZATION; IMAGE ANALYSIS; MOLECULAR DYNAMICS; MOTION; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE; X RAY;

BINDING SITES; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; X-RAY DIFFRACTION;

EID: 84874024456     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121635     Document Type: Article

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