@article{bibcite_311,
  keywords = {Protein Folding, molecular dynamics, Protein Engineering, Armadillo Domain Proteins, repeat proteins, spontaneous assembly},
  author = {R. P. Watson and M. T. Christen and C. Ewald and F. Bumbak and C. Reichen and M. Mihajlovic and E. Schmidt and P. G{\"u}ntert and A. Caflisch and A. Pl{\"u}ckthun and O. Zerbe},
  title = {Spontaneous self-assembly of engineered armadillo repeat protein fragments into a folded structure},
  abstract = {<p>Repeat proteins are built of modules, each of which constitutes a structural motif. We have investigated whether fragments of a designed consensus armadillo repeat protein (ArmRP) recognize each other. We examined a split ArmRP consisting of an N-capping repeat (denoted Y), three internal repeats (M), and a C-capping repeat (A). We demonstrate that the C-terminal MA fragment adopts a fold similar to the corresponding part of the entire protein. In contrast, the N-terminal YM<sub>2</sub> fragment constitutes a molten globule. The two fragments form a 1:1 YM<sub>2</sub>:MA complex with a nanomolar dissociation constant essentially identical to the crystal structure of the continuous YM<sub>3</sub>A protein. Molecular dynamics simulations show that the complex is structurally stable over a 1 \&mu;s timescale and reveal the importance of hydrophobic contacts across the interface. We propose that the existence of a stable complex recapitulates possible intermediates in the early evolution of these repeat proteins.</p>},
  year = {2014},
  journal = {Structure},
  volume = {22},
  pages = {985-995},
  month = {2014 Jul 8},
  issn = {1878-4186},
  doi = {10.1016/j.str.2014.05.002},
  language = {eng},
}