HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequence

Volume: 317, Issue: 3, Pages: 385 - 399
Published: Mar 1, 2002
Abstract
The nucleocapsid protein NCp7 of HIV-1 possesses a nucleic acid chaperone activity that is critical in minus and plus strand transfer during reverse transcription. The minus strand transfer notably relies on the ability of NCp7 to destabilize the stable stem with five contiguous, double-stranded segments of both the TAR sequence at the 3′ end of the viral genome and the complementary sequence, cTAR, in minus strong-stop DNA. In order to examine...
Paper Details
Title
HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequence
Published Date
Mar 1, 2002
Volume
317
Issue
3
Pages
385 - 399
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