The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold

Journal of Molecular Biology

Volumn 341, Issue 4, 2004, Pages 893-899

  Won, Hyung Sik ^a   Low, Lieh Yoon ^a   De Guzman, Roberto ^a   Martinez Yamout, Maria ^a   Jakob, Ursula ^b   Jane Dyson, H ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

NMR structure; oxidation reduction; oxidative stress; zinc cysteine coordination

Indexed keywords

CHAPERONE; CYSTEINE; HEAT SHOCK PROTEIN; ISOPROTEIN; LIGAND; RECOMBINANT PROTEIN; THIOL GROUP; ZINC;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; DISULFIDE BOND; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; STOICHIOMETRY;

ESCHERICHIA COLI;

EID: 3843102633     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.06.046     Document Type: Article

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