Auclair, Sarah M <br/><br/>
Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.  [electronic resource] 

 -  Biochemistry  Apr 2013 
 - 2388-401 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. 
<br/><br/><label>ISSN: </label>1520-4995 
<br/><br/><label>Standard No.: </label>10.1021/bi301217t  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphatases--chemistry<br/>Bacterial Proteins--chemistry<br/>Cysteine--chemistry<br/>Escherichia coli--chemistry<br/>Fluorescence Resonance Energy Transfer<br/>Membrane Transport Proteins--chemistry<br/>Models, Molecular<br/>Point Mutation<br/>Protein Binding<br/>Protein Conformation<br/>Protein Multimerization<br/>Protein Sorting Signals<br/>SEC Translocation Channels<br/>SecA Proteins