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Volumn 14, Issue 4, 2001, Pages 255-260
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A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli
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Author keywords
Molecular dynamic simulations; Protein engineering; Site directed mutagenesis; Thermostability; Thioredoxin
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Indexed keywords
ARGININE;
THIOREDOXIN;
ALICYCLOBACILLUS ACIDOCALDARIUS;
ARTICLE;
BACILLUS;
CIRCULAR DICHROISM;
ESCHERICHIA COLI;
GENETIC ENGINEERING;
HYDROGEN BOND;
MOLECULAR DYNAMICS;
MOLECULAR MODEL;
NONHUMAN;
POINT MUTATION;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN INTERACTION;
PROTEIN LOCALIZATION;
PROTEIN STABILITY;
SIMULATION;
SITE DIRECTED MUTAGENESIS;
SPECTROFLUOROMETRY;
THERMOSTABILITY;
ALICYCLOBACILLUS ACIDOCALDARIUS;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0034961587
PISSN: 02692139
EISSN: None
Source Type: Journal
DOI: 10.1093/protein/14.4.255 Document Type: Article |
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Times cited : (32)
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References (20)
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