The Structure of a Two-Disulfide Intermediate Assists in Elucidating the Oxidative Folding Pathway of a Cyclic Cystine Knot Protein

Structure

Volumn 16, Issue 6, 2008, Pages 842-851

  Cemazar, Maša ^a   Joshi, Ajinkya ^a   Daly, Norelle L ^a   Mark, Alan E ^a   Craik, David J ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

PROTEINS

Indexed keywords

DISULFIDE; VEGETABLE PROTEIN;

ARTICLE; CYSTINE KNOT MOTIF; DISULFIDE BOND; NONHUMAN; OXIDATION; PHYTOCHEMISTRY; PLANT SEED; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS;

COMPUTER SIMULATION; CYCLOTIDES; CYSTINE KNOT MOTIFS; DISULFIDES; ISOMERISM; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PLANT PROTEINS; PROTEIN FOLDING;

EID: 44649153789     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.02.023     Document Type: Article

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