Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques (Q36277950)

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English	Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques	scientific article

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scholarly article

1 reference

Europe PubMed Central

13 August 2017

Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques (English)

1 reference

Europe PubMed Central

13 August 2017

Escherichia coli

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phosphorylation

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author name string

J G Pelton

1

1 reference

Europe PubMed Central

13 August 2017

D A Torchia

2

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Europe PubMed Central

13 August 2017

N D Meadow

3

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Europe PubMed Central

13 August 2017

S Roseman

4

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Europe PubMed Central

13 August 2017

publication date

1 April 1993

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Europe PubMed Central

13 August 2017

Protein Science

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Europe PubMed Central

13 August 2017

2

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Europe PubMed Central

13 August 2017

4

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Europe PubMed Central

13 August 2017

543-558

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Europe PubMed Central

13 August 2017

Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

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Culture medium for enterobacteria

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Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria

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The role of the alpha-helix dipole in protein function and structure

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Tertiary structure of histidine-containing protein of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli

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30 September 2017

Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain

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Site-directed mutagenesis of the phosphocarrier protein. IIIGlc, a major signal-transducing protein in Escherichia coli

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Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy

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Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc

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Low resolution solution structure of theBacillus subtilisglucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy

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Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques.

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Modified assay procedures for the phosphotransferase system in enteric bacteria

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Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119

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Identifiers

10.1002/PRO.5560020406

1 reference

Europe PubMed Central

13 August 2017

1 reference

Europe PubMed Central

13 August 2017

1 reference

Europe PubMed Central

13 August 2017

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