The domains in gammaB-crystallin: identical fold-different stabilities.

@article{Mayr1997TheDI,
  title={The domains in gammaB-crystallin: identical fold-different stabilities.},
  author={E M Mayr and R. C. A. Jaenicke and Rudi Glockshuber},
  journal={Journal of molecular biology},
  year={1997},
  volume={269 2},
  pages={260-9}
}
gammaB-crystallin from vertebrate eye lens is an all beta-sheet two-domain protein with a high degree of intrachain symmetry. Its N and C-terminal domains show high levels of sequence similarity and structural identity. In natural gammaB-crystallin, the domains fold independently. The recombinantly expressed isolated domains are stable monomeric proteins, which do not associate spontaneously to form a gammaB-like dimer. In contrast to their identical folding topology, the two domains obviously… CONTINUE READING

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