Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.

@article{Sagermann1999StructuralCO,
  title={Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.},
  author={Martin Sagermann and W. A. Baase and Brian W. Matthews},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 11},
  pages={6078-83}
}
To test a different approach to understanding the relationship between the sequence of part of a protein and its conformation in the overall folded structure, the amino acid sequence corresponding to an alpha-helix of T4 lysozyme was duplicated in tandem. The presence of such a sequence repeat provides the protein with "choices" during folding. The mutant protein folds with almost wild-type stability, is active, and crystallizes in two different space groups, one isomorphous with wild type and… CONTINUE READING