Molecular dynamics simulation studies of a protein-RNA complex with a selectively modified binding interface.

@article{Zhao2006MolecularDS,
  title={Molecular dynamics simulation studies of a protein-RNA complex with a selectively modified binding interface.},
  author={Ying Zhao and Bethany L. Kormos and David L. Beveridge and Anne M. Baranger},
  journal={Biopolymers},
  year={2006},
  volume={81 4},
  pages={256-69}
}
The RNA recognition motif (RRM) is one of the most common RNA binding domains. We have investigated the contribution of three highly conserved aromatic amino acids to RNA binding by the N-terminal RRM of the U1A protein. Recently, we synthesized a modified base (A-4CPh) in which a phenyl group is tethered to adenine using a linker of 4 methylene groups. The substitution of this base for adenine in the target RNA selectively stabilizes the complex formed with a U1A protein in which one of the… CONTINUE READING