Exploring the repeat protein universe through computational protein design

Brunette Tj, Fabio Parmeggiani, Po-Ssu Huang, Gira Bhabha, Damian C. Ekiert, Susan E. Tsutakawa, Greg L. Hura, John A. Tainer and David Baker ()
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Brunette Tj: University of Washington
Fabio Parmeggiani: University of Washington
Po-Ssu Huang: University of Washington
Gira Bhabha: UCSF
Damian C. Ekiert: UCSF
Susan E. Tsutakawa: Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley National Laboratory
Greg L. Hura: Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley National Laboratory
John A. Tainer: Molecular Biophysics & Integrated Bioimaging, Lawrence Berkeley National Laboratory
David Baker: University of Washington

Nature, 2015, vol. 528, issue 7583, 580-584

Abstract: In this study, 83 proteins containing helix–loop–helix–loop repeats were designed—with sequences unrelated to known repeat proteins—and experimentally characterized; 43 solution X-ray scattering spectra and 15 structures of the designed proteins show that these non-natural repeat proteins have a broad range of curvatures and that their overall structures are in close agreement with design models.

Date: 2015
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DOI: 10.1038/nature16162

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