Kortemme, T <br/><br/>
Similarities between the spectrin SH3 domain denatured state and its folding transition state.  [electronic resource] 

 -  Journal of molecular biology  Apr 2000 
 - 1217-29 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.2000.3618  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acids--pharmacology<br/>Amino Acid Sequence<br/>Amino Acid Substitution--genetics<br/>Animals<br/>Chickens<br/>Deuterium--metabolism<br/>Drosophila Proteins<br/>Hydrogen-Ion Concentration<br/>Insect Proteins--chemistry<br/>Kinetics<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutation--genetics<br/>Nuclear Magnetic Resonance, Biomolecular<br/>Protein Denaturation--drug effects<br/>Protein Folding<br/>Protein Renaturation<br/>Protein Structure, Secondary--drug effects<br/>Protons<br/>Spectrin--chemistry<br/>Thermodynamics<br/>src Homology Domains--drug effects