HAL (France)
open access
Flexibility of the TRMT10C N-Terminal Domain Helix Explored by Molecular Dynamics Simulations
Abstract The human mitochondrial tRNA methyltransferase TRMT10C contains a 41-residue long positively charged α-helix in its N-terminal domain, interacting with tRNAs from the anticodon to the T-loops. Here, we investigated the flexibility of this N-terminal long α-helix using comparative molecular
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