Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer. [electronic resource]
Producer: 20130529Description: 2388-401 p. digitalISSN:- 1520-4995
- Adenosine Triphosphatases -- chemistry
- Bacterial Proteins -- chemistry
- Cysteine -- chemistry
- Escherichia coli -- chemistry
- Fluorescence Resonance Energy Transfer
- Membrane Transport Proteins -- chemistry
- Models, Molecular
- Point Mutation
- Protein Binding
- Protein Conformation
- Protein Multimerization
- Protein Sorting Signals
- SEC Translocation Channels
- SecA Proteins
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
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