Carvalho, Sofia B <br/><br/>
Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.  [electronic resource] 

 -  PloS one  2013 
 - e76629 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1932-6203 
<br/><br/><label>Standard No.: </label>10.1371/journal.pone.0076629  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Computer Simulation<br/>Flocculation<br/>Humans<br/>Hydrogen-Ion Concentration<br/>Hydrophobic and Hydrophilic Interactions<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Peptide Mapping<br/>Protein Folding<br/>Protein Stability<br/>Protein Structure, Quaternary<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Recombinant Proteins--chemistry<br/>S100 Proteins--chemistry<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid