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Volumn 1545, Issue 1-2, 2001, Pages 227-237
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The chaperone-like activity of a small heat shock protein is lost after sulfoxidation of conserved methionines in a surface-exposed amphipathic α-helix
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Author keywords
Amphipathic helix; Chaperone; Methionine sulfoxidation; Oligomer; Small heat shock protein
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Indexed keywords
CHAPERONE;
HEAT SHOCK PROTEIN;
HEAT SHOCK PROTEIN 21;
METHIONINE;
UNCLASSIFIED DRUG;
ALPHA HELIX;
ARTICLE;
CHLOROPLAST;
CIRCULAR DICHROISM;
ENZYME ACTIVITY;
OXIDATIVE STRESS;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN DEGRADATION;
PROTEIN MODIFICATION;
PROTEIN MOTIF;
AMINO ACID SEQUENCE;
ARABIDOPSIS;
ARABIDOPSIS PROTEINS;
CHLOROPLASTS;
CHROMATOGRAPHY, GEL;
CIRCULAR DICHROISM;
CITRATE (SI)-SYNTHASE;
HEAT-SHOCK PROTEINS;
INSULIN;
METHIONINE;
MOLECULAR SEQUENCE DATA;
OXIDATION-REDUCTION;
OXIDATIVE STRESS;
PEPTIDE MAPPING;
PLANT PROTEINS;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN PROCESSING, POST-TRANSLATIONAL;
RECOMBINANT FUSION PROTEINS;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
SULFUR;
THERMODYNAMICS;
EMBRYOPHYTA;
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EID: 0035830637
PISSN: 01674838
EISSN: None
Source Type: Journal
DOI: 10.1016/S0167-4838(00)00280-6 Document Type: Article |
Times cited : (38)
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References (42)
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