Solution structure and dynamics of a de novo designed three-helix bundle protein.

@article{Walsh1999SolutionSA,
  title={Solution structure and dynamics of a de novo designed three-helix bundle protein.},
  author={Scott T. R. Walsh and Hong Cheng and James W. Bryson and Heinrich Roder and William F. DeGrado},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 10},
  pages={
          5486-91
        }
}
  • Scott T. R. Walsh, Hong Cheng, +2 authors William F. DeGrado
  • Published 1999
  • Medicine, Biology
  • Proceedings of the National Academy of Sciences of the United States of America
  • Although de novo protein design is an important endeavor with implications for understanding protein folding, until now, structures have been determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported. The structure of alpha3D was not based on any natural protein, and yet it shows thermodynamic and spectroscopic properties typical of native proteins. A variety of features contribute… CONTINUE READING

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