(Q28252823)

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Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity

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Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity (English)

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Salmonella Typhimurium

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Salmonella typhimurium

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K Nikaido

1

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P Q Liu

2

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G F Ames

3

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language of work or name

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publication date

31 October 1997

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Journal of Biological Chemistry

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272

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44

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27745-52

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1 reference

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Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter).

1 reference

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Structural model of the nucleotide-binding conserved component of periplasmic permeases

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Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

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Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation

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Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide.

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Circular dichroic analysis of protein conformation: inclusion of the beta-turns.

1 reference

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Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form

1 reference

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A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

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UPTAKE OF AMINO ACIDS BY SALMONELLA TYPHIMURIUM.

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Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium

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