The possible roles of residues 79 and 80 of the Trp repressor from Escherichia coli K-12 in trp operator recognition
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics,Molecular Biology
Link
http://link.springer.com/content/pdf/10.1007/BF00294681.pdf
Reference66 articles.
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2. Anderson JE, Ptashne M, Harrison SC (1987) Structure of the repressor-operator complex of bacteriophage 434. Nature 326:846–852
3. Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW (1981) Structure of the cro repressor from bacteriophage λ and its interaction with DNA. Nature 290:754–758
4. Arakawa T, Bhat R, Timasheff SN (1990) Why preferential hydration does not always stabilise the native structure of globular proteins. Biochemistry 29:1924–1931
5. Arrowsmith CH, Carey J, Treat-Clemons L, Jardetzky O (1989) NMR assignments for the amino terminal residues of Trp repressor and their role in DNA binding. Biochemistry 28:3875–3879
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1. Mutational Analysis of Conserved Residues in the Putative DNA-Binding Domain of the Response Regulator Spo0A of Bacillus subtilis;Journal of Bacteriology;2000-12-15
2. Repressor assembly at trp binding sites is dependent on the identity of the intervening dinucleotide between the binding half sites;Journal of Molecular Biology;1997-03
3. Mutants in position 69 of the Trp repressor ofEscherichia coli K12 with altered DNA-binding specificity;Molecular and General Genetics MGG;1996-06
4. Co-operative binding of two Trp repressor dimers to ?- or ?-centred trp operators;Molecular Microbiology;1996-04
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