Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens.

@article{Palme1997MutationalAO,
  title={Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens.},
  author={Stefan Palme and Christine Slingsby and Ruprecht Jaenicke},
  journal={Protein science : a publication of the Protein Society},
  year={1997},
  volume={6 7},
  pages={
          1529-36
        }
}
gamma B-crystallin is a monomeric member of the beta gamma-superfamily of vertebrate eye lens proteins. It consists of two similar domains with all-beta Greek key topology associating about an approximate two-fold axis. At pH 2, with urea as the denaturant, the domains show independent equilibrium unfolding transitions, suggesting different intrinsic stabilities. Denaturation experiments using recombinant one- or two-domain proteins showed that the N-terminal domain on its own exhibits… CONTINUE READING
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