Hellstrand, Erik <br/><br/>
Förster resonance energy transfer studies of calmodulin produced by native protein ligation reveal inter-domain electrostatic repulsion.  [electronic resource] 

 -  The FEBS journal  Jun 2013 
 - 2675-87 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1742-4658 
<br/><br/><label>Standard No.: </label>10.1111/febs.12269  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Binding Sites<br/>Calcium--chemistry<br/>Calcium Signaling<br/>Calmodulin--chemistry<br/>Fluorescence Resonance Energy Transfer<br/>Fluorescent Dyes--chemistry<br/>Humans<br/>Maleimides--chemistry<br/>Models, Molecular<br/>Osmolar Concentration<br/>Peptide Fragments--chemistry<br/>Protein Conformation<br/>Protein Denaturation<br/>Protein Structure, Tertiary<br/>Quinolinium Compounds--chemistry<br/>Static Electricity