Literature summary for 3.1.26.13 extracted from

Kern, G.; Handel, T.; Marqusee, S.
Characterization of a folding intermediate from HIV-1 ribonuclease H (1998), Protein Sci., 7, 2164-2174.

Search for more literature for 3.1.26.13

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the isolated RNase H domain in Escherichia coli	Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of the kinetic refolding intermediate using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
Refolding of the isolated HIV RNase H domain shows a kinetic intermediate detectable by stopped-flow far UV circular dichroism and pulse-labeling H/D exchange. In this intermediate, strands 1, 4, and 5 as well as helices A and D appear to be structured. Compared to its homolog from Escherichia coli, the rate limiting step in refolding of HIV RNase H appears closer to the native state. This kinetic intermediate has been modeled using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability	Human immunodeficiency virus 1

Renatured (Comment)

Organism

Refolding of the isolated HIV RNase H domain shows a kinetic intermediate detectable by stopped-flow far UV circular dichroism and pulse-labeling H/D exchange. In this intermediate, strands 1, 4, and 5 as well as helices A and D appear to be structured. Compared to its homolog from Escherichia coli, the rate limiting step in refolding of HIV RNase H appears closer to the native state. This kinetic intermediate has been modeled using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability

Human immunodeficiency virus 1

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Release 2023.1 (January 2023)