Liang, Fu-Cheng <br/><br/>
Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.  [electronic resource] 

 -  Proceedings of the National Academy of Sciences of the United States of America  Mar 2016 
 - E1615-24 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1091-6490 
<br/><br/><label>Standard No.: </label>10.1073/pnas.1524777113  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Arabidopsis--metabolism<br/>Arabidopsis Proteins--chemistry<br/>Binding Sites<br/>Chloroplast Proteins--chemistry<br/>Light-Harvesting Protein Complexes--metabolism<br/>Membrane Proteins--metabolism<br/>Models, Molecular<br/>Molecular Chaperones--metabolism<br/>Molecular Sequence Data<br/>Nuclear Magnetic Resonance, Biomolecular<br/>Protein Binding<br/>Protein Conformation<br/>Protein Interaction Mapping<br/>Protein Structure, Tertiary<br/>Recombinant Fusion Proteins--metabolism<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Signal Recognition Particle--chemistry<br/>Solubility<br/>Structure-Activity Relationship<br/>Thylakoid Membrane Proteins--metabolism<br/>Thylakoids--metabolism