HIV-1 gp41 and gp160 are hyperthermostable proteins in a mesophilic environment. Characterization of gp41 mutants.

@article{Krell2004HIV1GA,
  title={HIV-1 gp41 and gp160 are hyperthermostable proteins in a mesophilic environment. Characterization of gp41 mutants.},
  author={Tino Krell and Fr{\'e}d{\'e}ric Gr{\'e}co and Olivier Engel and Jean Dubayle and Joseline Dubayle and Audrey Kennel and Benoit B Charloteaux and R. Brasseur and Michel Chevalier and R{\'e}gis Sodoyer and Rapha{\"e}lle El Habib},
  journal={European journal of biochemistry},
  year={2004},
  volume={271 8},
  pages={1566-79}
}
HIV gp41(24-157) unfolds cooperatively over the pH range of 1.0-4.0 with T(m) values of > 100 degrees C. At pH 2.8, protein unfolding was 80% reversible and the DeltaH(vH)/DeltaH(cal) ratio of 3.7 is indicative of gp41 being trimeric. No evidence for a monomer-trimer equilibrium in the concentration range of 0.3-36 micro m was obtained by DSC and tryptophan fluorescence. Glycosylation of gp41 was found to have only a marginal impact on the thermal stability. Reduction of the disulfide bond or… CONTINUE READING