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Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY

Biochemistry

Nov 30, 1993

Vladimir V FilimonovLuis A Serrano

PMID: 8251514

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Abstract

CheY, the 129 amino acid chemotactic protein from Escherichia coli, is a good model for studies of folding of parallel alpha/beta proteins. We report here the thermodynamic characterization of the wild-type CheY at different pH values and in different buffers and denaturation conditions...read more

Mentioned in this Paper

Thermodynamics
Tertiary Protein Structure
Fluorescence Spectroscopy
Mutagenesis Process
Ampholytes
Cell Surface Proteins
Circular Dichroism, Vibrational
Protein Folding, Globular
1-anilino-8-naphthalenesulfonate, magnesium (2: 1)
Anilino Naphthalenesulfonates
Paper Details
References
  • References37
  • Citations31
1234
  • References37
  • Citations31
1234

Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY

Biochemistry

Nov 30, 1993

Vladimir V FilimonovLuis A Serrano

PMID: 8251514

DOI:

Abstract

CheY, the 129 amino acid chemotactic protein from Escherichia coli, is a good model for studies of folding of parallel alpha/beta proteins. We report here the thermodynamic characterization of the wild-type CheY at different pH values and in different buffers and denaturation conditions...read more

Mentioned in this Paper

Thermodynamics
Tertiary Protein Structure
Fluorescence Spectroscopy
Mutagenesis Process
Ampholytes

Related Papers

Paper Details
References
  • References37
  • Citations31
1234
  • References37
  • Citations31
1234

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