NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B. [electronic resource]
Producer: 20171121Description: 18024-18043 p. digitalISSN:- 1083-351X
- Allosteric Regulation -- drug effects
- Allosteric Site -- drug effects
- Antiviral Agents -- chemistry
- Enzyme Inhibitors -- chemistry
- Gene Deletion
- Hepacivirus -- enzymology
- Intrinsically Disordered Proteins -- chemistry
- Isoleucine -- chemistry
- Models, Molecular
- Mutagenesis, Site-Directed
- Nuclear Magnetic Resonance, Biomolecular
- Oligoribonucleotides -- chemistry
- Peptide Fragments -- antagonists & inhibitors
- Point Mutation
- Protein Conformation
- Protein Interaction Domains and Motifs
- Protein Refolding -- drug effects
- Pyrones -- chemistry
- RNA-Dependent RNA Polymerase -- antagonists & inhibitors
- Recombinant Proteins -- chemistry
- Solubility
- Triazoles -- chemistry
- Viral Nonstructural Proteins -- antagonists & inhibitors
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Publication Type: Journal Article
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