High mobility of carboxyl-terminal region of bacterial chemotaxis phosphatase CheZ is diminished upon binding divalent cation or CheY-P substrate. [electronic resource]
Producer: 20050816Description: 7768-76 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Bacterial Proteins -- antagonists & inhibitors
- Beryllium -- metabolism
- Binding Sites
- Cations, Divalent -- chemistry
- Chemotaxis
- Escherichia coli Proteins
- Fluorescein -- metabolism
- Fluorescence Polarization
- Fluorescence Resonance Energy Transfer
- Fluorides -- metabolism
- Magnesium Chloride -- chemistry
- Membrane Proteins -- antagonists & inhibitors
- Methyl-Accepting Chemotaxis Proteins
- Molecular Motor Proteins -- antagonists & inhibitors
- Molecular Sequence Data
- Peptide Fragments -- antagonists & inhibitors
- Phosphoric Monoester Hydrolases -- antagonists & inhibitors
- Protein Structure, Tertiary
- Substrate Specificity
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
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