Mabbutt, B C <br/><br/>
NMR studies of oxyleghemoglobin: assignment of distal histidine proton resonances and evidence for pH-dependent changes in conformation.  [electronic resource] 

 -  Biochimica et biophysica acta  Dec 1983 
 - 281-8 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-3002 
<br/><br/><label>Standard No.: </label>10.1016/0167-4838(83)90237-6  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Histidine--chemistry<br/>Hydrogen-Ion Concentration<br/>Leghemoglobin--analogs & derivatives<br/>Nuclear Magnetic Resonance, Biomolecular<br/>Oxygen--chemistry<br/>Protein Conformation<br/>Protons<br/>Glycine max--chemistry