Structural rearrangements near the chromophore influence the maturation speed and brightness of DsRed variants.

  title={Structural rearrangements near the chromophore influence the maturation speed and brightness of DsRed variants.},
  author={Daniel E Strongin and Brooke J. Bevis and Nhi Y Khuong and Maureen E. Downing and Rita L. Strack and Karthik Sundaram and Benjamin S. Glick and Robert J. Keenan},
  journal={Protein engineering, design & selection : PEDS},
  volume={20 11},
The red fluorescent protein DsRed has been extensively engineered for use as an in vivo research tool. In fast maturing DsRed variants, the chromophore maturation half-time is approximately 40 min, compared to approximately 12 h for wild-type DsRed. Further, DsRed has been converted from a tetramer into a monomer, a task that entailed mutating approximately 20% of the amino acids. These engineered variants of DsRed have proven extremely valuable for biomedical research, but the structural basis… CONTINUE READING

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