Ontology highlight
ABSTRACT:
SUBMITTER: Dunn LL
PROVIDER: S-EPMC3804327 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
Dunn Linda L LL Boyer Paul L PL Clark Patrick K PK Hughes Stephen H SH
Virology 20130711 1-2
Previous work on mutations in the thumb of HIV-1 reverse transcriptase (RT) showed that the majority of the mutant RTs were degraded (by the viral protease) to various extents in virions. This degradation was, in most cases, temperature sensitive, and presumably was due to a partial unfolding of the protein at 37°C. We used recombinant proteins to investigate the effects of the mutations on the thermal stability and proteolytic degradation of RT. Both subunits contribute to the stability of RT. ...[more]