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Volumn 487, Issue 3, 2001, Pages 372-376
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The membrane-extrinsic domain of cytochrome b558/566 from the Archaeon Sulfolobus acidocaldarius performs pivoting movements with respect to the membrane surface
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Author keywords
Archaeon; Cytochrome b558 566; Cytochrome cy; Electron paramagnetic resonance; Sulfolobus
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Indexed keywords
CYTOCHROME B;
CYTOCHROME B558;
CYTOCHROME B566;
GLYCOSYLATED PROTEIN;
METHIONINE;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
AMINO TERMINAL SEQUENCE;
ANISOTROPY;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CELL MEMBRANE;
CONTROLLED STUDY;
ELECTRON SPIN RESONANCE;
ELECTRON TRANSPORT;
NONHUMAN;
OXIDATION REDUCTION POTENTIAL;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN PURIFICATION;
PROTEIN STRUCTURE;
SULFOLOBUS ACIDOCALDARIUS;
AMINO ACID SEQUENCE;
CELL MEMBRANE;
CYTOCHROME B GROUP;
ELECTRON SPIN RESONANCE SPECTROSCOPY;
ELECTRON TRANSPORT;
MOLECULAR SEQUENCE DATA;
NADPH OXIDASE;
OXIDATION-REDUCTION;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
SULFOLOBUS;
SULFOLOBUS ACIDOCALDARIUS;
ARCHAEA;
SULFOLOBUS;
SULFOLOBUS ACIDOCALDARIUS;
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EID: 0035808256
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(00)02357-7 Document Type: Article |
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Times cited : (16)
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References (35)
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