Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins. [electronic resource]
Producer: 20140429Description: e76629 p. digitalISSN:- 1932-6203
- 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
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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