Seigneuret, M <br/><br/>
High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin.  [electronic resource] 

 -  Biochemistry  Apr 1991 
 - 3885-92 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi00230a012  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Bacteriorhodopsins--chemistry<br/>Carbon Isotopes<br/>Detergents<br/>Halobacterium--metabolism<br/>Isotope Labeling<br/>Kinetics<br/>Liposomes<br/>Magnetic Resonance Spectroscopy--methods<br/>Methionine<br/>Models, Structural<br/>Molecular Sequence Data<br/>Papain--metabolism<br/>Protein Conformation<br/>Solubility<br/>Spin Labels<br/>Thermodynamics