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Literature summary for 3.1.26.4 extracted from
- A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble (2009), J. Mol. Biol., 391, 461-470.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| I25A | large destabilization, compared to wild-type. Mutant is active and retains a native-like fold. Mutation results in the equilibrium population of the folding intermediate under near-native conditions. The intermediate is undetectable in a series of heteronuclear single quantum coherences, revealing the dynamic nature of this partially unfolded form on the timescale of NMR detection | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A7Y4 | - |
- |
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Release 2023.1 (January 2023)
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