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Literature DB >> 3045823

Tryptophan repressor of Escherichia coli shows unusual thermal stability.

S J Bae¹, W Y Chou, K Matthews, J M Sturtevant.

Abstract

Differential scanning calorimetry demonstrates that the tryptophan repressor of Escherichia coli is unusually resistant to thermal denaturation. The dimeric protein undergoes reversible dissociative unfolding at pH 7.5 centered at about 90 degrees C. The thermal stability may be due in part to the unusual structure of the protein, which is composed of two identical intertwined polypeptide chains.

Entities: Chemical Species

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Year: 1988 PMID： 3045823 PMCID： PMC282051 DOI： 10.1073/pnas.85.18.6731

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

5 in total

1. High level production and rapid purification of the E. coli trp repressor.

Authors: J L Paluh; C Yanofsky
Journal: Nucleic Acids Res Date: 1986-10-24 Impact factor: 16.971

2. Thermal denaturation of the core protein of lac repressor.

Authors: S P Manly; K S Matthews; J M Sturtevant
Journal: Biochemistry Date: 1985-07-16 Impact factor: 3.162

3. The three-dimensional structure of trp repressor.

Authors: R W Schevitz; Z Otwinowski; A Joachimiak; C L Lawson; P B Sigler
Journal: Nature Date: 1985 Oct 31-Nov 6 Impact factor: 49.962

4. Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor.

Authors: R P Gunsalus; C Yanofsky
Journal: Proc Natl Acad Sci U S A Date: 1980-12 Impact factor: 11.205

5. Functional inferences from crystals of Escherichia coli trp repressor.

Authors: A Joachimiak; R W Schevitz; R L Kelley; C Yanofsky; P B Sigler
Journal: J Biol Chem Date: 1983-10-25 Impact factor: 5.157

5 in total

3 in total

Tryptophan repressor of Escherichia coli shows unusual thermal stability.

1. High level production and rapid purification of the E. coli trp repressor.

2. Thermal denaturation of the core protein of lac repressor.

3. The three-dimensional structure of trp repressor.

4. Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor.

5. Functional inferences from crystals of Escherichia coli trp repressor.

1. Type III secretion system effector proteins are mechanically labile.

2. Environment-dependent long-range structural distortion in a temperature-sensitive point mutant.

3. Mutant tryptophan aporepressors with altered specificities of corepressor recognition.