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 a...
Topics
- Circular Dichroism
- Deuterium
- Drug Design
- Enzyme Inhibitors
- Enzyme Stability
- Guanidine
- HIV-1
- Hydrogen
- Kinetics
- Models, Molecular
- Mutation
- Protein Denaturation
- Protein Folding
- Protein Structure, Secondary
- Ribonuclease H
- Viral Proteins