Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability.

@article{Delbrck2001CrystalSO,
  title={Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability.},
  author={Heinrich Delbr{\"u}ck and Uwe C. Mueller and Dieter Perl and Franz Xaver Schmid and Udo Heinemann},
  journal={Journal of molecular biology},
  year={2001},
  volume={313 2},
  pages={359-69}
}
The cold shock proteins Bc-Csp from the thermophile Bacillus caldolyticus and Bs-CspB from the mesophile Bacillus subtilis differ significantly in their conformational stability, although the two proteins differ by only 12 out of 67 amino acid residues. The three-dimensional structure of these small and compact beta-barrel proteins without disulfide bonds, cis-proline residues or tightly bound cofactors is very similar. Previous work has shown that Bc-Csp displays a twofold increase in the free… CONTINUE READING

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