Domke, T <br/><br/>
Birch pollen profilin: structural organization and interaction with poly-(L-proline) peptides as revealed by NMR.  [electronic resource] 

 -  FEBS letters  Jul 1997 
 - 291-5 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0014-5793 
<br/><br/><label>Standard No.: </label>10.1016/s0014-5793(97)00719-9  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acanthamoeba--chemistry<br/>Amino Acid Sequence<br/>Animals<br/>Binding Sites<br/>Cell Adhesion Molecules--metabolism<br/>Cloning, Molecular<br/>Contractile Proteins<br/>Cytoskeletal Proteins<br/>Escherichia coli<br/>Magnetic Resonance Spectroscopy<br/>Microfilament Proteins--chemistry<br/>Molecular Sequence Data<br/>Peptides--metabolism<br/>Phosphoproteins--metabolism<br/>Plant Proteins--chemistry<br/>Pollen--chemistry<br/>Profilins<br/>Protein Binding<br/>Protein Structure, Secondary<br/>Proteins--metabolism<br/>Recombinant Proteins--chemistry<br/>Trees<br/>Vasodilator-Stimulated Phosphoprotein