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Article

Characterization of a folding intermediate from HIV-1 ribonuclease H.

Protein science : a publication of the Protein Society - 1 Oct 1998

Kern G, Handel T, Marqusee S

Abstract excerpt

The RNase H domain from HIV-1 (HIV RNase H) encodes an essential retroviral activity. 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...

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Identifiers

PMID: 9792104
DOI: 10.1002/pro.5560071014
PMCID: PMC2143833

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