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Volumn 41, Issue 19, 2002, Pages 6193-6201
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Pyrococcus furiosus α-amylase is stabilized by calcium and zinc
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Author keywords
[No Author keywords available]
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Indexed keywords
POTENTIAL FUNCTION;
AMINO ACIDS;
BACTERIA;
CALCIUM;
EMISSION SPECTROSCOPY;
ENZYMES;
THERMODYNAMIC STABILITY;
ZINC;
BIOCHEMISTRY;
AMYLASE;
CALCIUM ION;
DITHIOTHREITOL;
EDETIC ACID;
METAL COMPLEX;
ZINC ION;
ARTICLE;
ATOMIC EMISSION SPECTROMETRY;
CALCIUM BINDING;
CONTROLLED STUDY;
ENZYME LOCALIZATION;
ENZYME STABILITY;
EXTRACELLULAR SPACE;
HIGH TEMPERATURE;
METAL BINDING;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN FAMILY;
PYROCOCCUS FURIOSUS;
THERMOPHILIC BACTERIUM;
THERMOSTABILITY;
ALPHA-AMYLASE;
AMINO ACID SUBSTITUTION;
BINDING SITES;
CALCIUM;
CYSTEINE;
ENZYME STABILITY;
LIGANDS;
MODELS, MOLECULAR;
MOLECULAR WEIGHT;
MUTAGENESIS, SITE-DIRECTED;
OXIDATION-REDUCTION;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PYROCOCCUS FURIOSUS;
RECOMBINANT PROTEINS;
TEMPERATURE;
ZINC;
ACTINOBACTERIA (CLASS);
ARCHAEA;
BACILLUS LICHENIFORMIS;
BACTERIA (MICROORGANISMS);
PYROCOCCUS;
PYROCOCCUS FURIOSUS;
THERMOCOCCUS KODAKARAENSIS;
UNCULTURED ACTINOMYCETE;
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EID: 0037076543
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi012106s Document Type: Article |
Times cited : (77)
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References (31)
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