Protein dynamics in a family of laboratory evolved thermophilic enzymes.

@article{Wintrode2003ProteinDI,
  title={Protein dynamics in a family of laboratory evolved thermophilic enzymes.},
  author={Patrick L. Wintrode and Deqiang Zhang and Nagarajan Vaidehi and Frances H. Arnold and William A. Goddard},
  journal={Journal of molecular biology},
  year={2003},
  volume={327 3},
  pages={745-57}
}
Molecular dynamics simulations were employed to study how protein solution structure and dynamics are affected by adaptation to high temperature. Simulations were carried out on a para-nitrobenzyl esterase (484 residues) and two thermostable variants that were generated by laboratory evolution. Although these variants display much higher melting temperatures than wild-type (up to 18 degrees C higher) they are both >97% identical in sequence to the wild-type. In simulations at 300 K the… CONTINUE READING