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Volumn 40, Issue 29, 2001, Pages 8531-8535
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Elongation factor Ts can act as a steric chaperone by increasing the solubility of nucleotide binding-impaired elongation factor-Tu
a,b
a,c
d
a
c
TNO
(Netherlands)
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Author keywords
[No Author keywords available]
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Indexed keywords
ELONGATION FACTOR;
CELLS;
ESCHERICHIA COLI;
GROWTH KINETICS;
MUTAGENS;
ELONGATION FACTOR TS;
ELONGATION FACTOR TU;
NUCLEOTIDE;
ARTICLE;
BINDING AFFINITY;
CELL GROWTH;
CHEMICAL STRUCTURE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN EXPRESSION;
PROTEIN FOLDING;
SOLUBILITY;
STEREOSPECIFICITY;
ESCHERICHIA COLI;
GLUTATHIONE TRANSFERASE;
GROWTH INHIBITORS;
GUANINE NUCLEOTIDES;
MOLECULAR CHAPERONES;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE ELONGATION FACTOR TU;
PEPTIDE ELONGATION FACTORS;
PLASMIDS;
PROTEIN BINDING;
PROTEIN FOLDING;
RECOMBINANT FUSION PROTEINS;
RIBONUCLEOSIDES;
SOLUBILITY;
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EID: 0035943021
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0104930 Document Type: Article |
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Times cited : (26)
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References (20)
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