Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release. [electronic resource]
Producer: 20160822Description: E1615-24 p. digitalISSN:- 1091-6490
- Amino Acid Sequence
- Arabidopsis -- metabolism
- Arabidopsis Proteins -- chemistry
- Binding Sites
- Chloroplast Proteins -- chemistry
- Light-Harvesting Protein Complexes -- metabolism
- Membrane Proteins -- metabolism
- Models, Molecular
- Molecular Chaperones -- metabolism
- Molecular Sequence Data
- Nuclear Magnetic Resonance, Biomolecular
- Protein Binding
- Protein Conformation
- Protein Interaction Mapping
- Protein Structure, Tertiary
- Recombinant Fusion Proteins -- metabolism
- Sequence Alignment
- Sequence Homology, Amino Acid
- Signal Recognition Particle -- chemistry
- Solubility
- Structure-Activity Relationship
- Thylakoid Membrane Proteins -- metabolism
- Thylakoids -- metabolism
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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