Conformation and stability of recombinant HIV-1 capsid protein p24 (rp24).

@article{Misselwitz1995ConformationAS,
  title={Conformation and stability of recombinant HIV-1 capsid protein p24 (rp24).},
  author={Rolf Misselwitz and Gert Hausdorf and Karin Welfle and W. E. H{\"o}hne and Heinz Welfle},
  journal={Biochimica et biophysica acta},
  year={1995},
  volume={1250 1},
  pages={9-18}
}
Conformation and stability of the recombinant protein HIV-1 rp24 were analyzed by circular dichroism, fluorescence spectroscopy and differential scanning calorimetry under different solvent conditions. From circular dichroism measurements, HIV-1 rp24 at pH 5.8 can be classified as an all alpha-helical protein. A fluorescence maximum of about 330 nm indicates a predominantly hydrophobic environment of the five tryptophan residues. The GdnHCl-induced unfolding curves monitored by CD and… CONTINUE READING