Literature summary for 3.1.26.4 extracted from

Connell, K.B.; Miller, E.J.; Marqusee, S.
The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms (2009), J. Mol. Biol., 391, 450-460.

Protein Variants

Protein Variants	Comment	Organism
D10A	mutation relieves charge repulsion in the periphery of the protein and stabilizes the protein by more than 3 kcal/mol. Comparison with mutant D10A/I53D, reference protein for three-state folding	Escherichia coli
D10A/I53D	mutations simultaneously destabilize the core and stabilize the periphery of the protein. Comparison with stabilized mutant D10A, reference protein for two-state folding	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
comparison of the folding trajectories of the three-state RNase H mutant D10A and the two-state RNase H mutant D10A/I53D, proteins with the same native-state topology but altered regional stability. Both versions of RNase H fold through a similar trajectory with similar high-energy conformations. Mutations in the core and the periphery of the protein affect similar aspects of folding for both variants	Escherichia coli

Renatured (Comment)

Organism

comparison of the folding trajectories of the three-state RNase H mutant D10A and the two-state RNase H mutant D10A/I53D, proteins with the same native-state topology but altered regional stability. Both versions of RNase H fold through a similar trajectory with similar high-energy conformations. Mutations in the core and the periphery of the protein affect similar aspects of folding for both variants

Escherichia coli

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Release 2023.1 (January 2023)