Extensive molecular dynamics simulations showing that canonical G8 and protonated A38H+ forms are most consistent with crystal structures of hairpin ribozyme.

@article{Mlnsk2010ExtensiveMD,
  title={Extensive molecular dynamics simulations showing that canonical G8 and protonated A38H+ forms are most consistent with crystal structures of hairpin ribozyme.},
  author={Vojtěch Ml{\'y}nsk{\'y} and Pavel Ban{\'a}{\vs} and Daniel Hollas and Kamila R{\'e}blov{\'a} and Nils G Walter and Jiř{\'i} {\vS}poner and Michal Otyepka},
  journal={The journal of physical chemistry. B},
  year={2010},
  volume={114 19},
  pages={6642-52}
}
The hairpin ribozyme is a prominent member of the group of small catalytic RNAs (RNA enzymes or ribozymes) because it does not require metal ions to achieve catalysis. Biochemical and structural data have implicated guanine 8 (G8) and adenine 38 (A38) as catalytic participants in cleavage and ligation catalyzed by the hairpin ribozyme, yet their exact role in catalysis remains disputed. To gain insight into dynamics in the active site of a minimal self-cleaving hairpin ribozyme, we have… CONTINUE READING
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