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Volumn 40, Issue 34, 2001, Pages 10047-10053
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Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity
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Author keywords
[No Author keywords available]
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Indexed keywords
LOW-ENERGY STRUCTURES;
ESCHERICHIA COLI;
HYDROGEN BONDS;
HYDROPHOBICITY;
MUTAGENESIS;
NUCLEAR MAGNETIC RESONANCE;
PROTEINS;
MUTANT PROTEIN;
PROTEIN;
THIOREDOXIN;
ARTICLE;
CONTROLLED STUDY;
ESCHERICHIA COLI;
HYDROGEN BOND;
HYDROPHOBICITY;
MUTAGENESIS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN FOLDING;
PROTEIN PURIFICATION;
PROTEIN STRUCTURE;
THERMODYNAMICS;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
CALORIMETRY, DIFFERENTIAL SCANNING;
CIRCULAR DICHROISM;
COMPUTER SIMULATION;
ESCHERICHIA COLI;
HYDROGEN BONDING;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
RECOMBINANT PROTEINS;
SPECTROMETRY, FLUORESCENCE;
THIOREDOXIN;
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EID: 0035964177
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi010427y Document Type: Article |
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Times cited : (39)
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References (49)
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