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Volumn 280, Issue 7, 2005, Pages 5527-5532
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Five amino acid residues responsible for the high stability of Hydrogenobacter thermophilus cytochrome c552: Reciprocal mutation analysis
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Author keywords
[No Author keywords available]
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Indexed keywords
BACTERIA;
CYTOLOGY;
HYDROCHLORIC ACID;
MUTAGENESIS;
PROTEINS;
REACTION KINETICS;
CYTOCHROMES;
HYDROGENOBACTER THERMOPHILUS;
THERMAL DENATURATION;
THERMOPHILIC BACTERIUM;
AMINO ACIDS;
AMINO ACID;
CYTOCHROME;
CYTOCHROME C552;
UNCLASSIFIED DRUG;
ARTICLE;
CONTROLLED STUDY;
DNA DENATURATION;
EVALUATION;
GENE MUTATION;
GRAM NEGATIVE BACTERIUM;
HYDROGENOBACTER THERMOPHILUS;
INTERMETHOD COMPARISON;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN STABILITY;
PSEUDOMONAS AERUGINOSA;
SEQUENCE HOMOLOGY;
THERMAL ANALYSIS;
AMINO ACIDS;
BACTERIA;
CIRCULAR DICHROISM;
CYTOCHROME C GROUP;
ELECTROCHEMISTRY;
ENZYME STABILITY;
ESCHERICHIA COLI;
GUANIDINE;
MAGNETIC RESONANCE SPECTROSCOPY;
MUTATION;
PERIPLASM;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
TEMPERATURE;
THERMODYNAMICS;
BACTERIA (MICROORGANISMS);
HYDROGENOBACTER THERMOPHILUS;
NEGIBACTERIA;
PSEUDOMONAS;
PSEUDOMONAS AERUGINOSA;
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EID: 20044389280
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M412392200 Document Type: Article |
Times cited : (34)
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References (24)
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