Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.

Carvalho, Sofia B

Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins. [electronic resource] - PloS one 2013 - e76629 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1932-6203

10.1371/journal.pone.0076629 doi


Amino Acid Sequence
Computer Simulation
Flocculation
Humans
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Molecular Sequence Data
Peptide Mapping
Protein Folding
Protein Stability
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins--chemistry
S100 Proteins--chemistry
Sequence Alignment
Sequence Homology, Amino Acid