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Non-canonical amino acids (N AA ), as building blocks for peptides and proteins during ribosomal translation, represent a nearly infinite supply of novel functions. The specific selection, activation and tRNA-charging of amino acids by aminoacyl-tRNA synthetases (AARS) in the aminoacylation reaction are essential steps. In most cases, aminoacylation of N AA  is a good indication that the related amino acid will participate in ribosomal translation as well. However, testing the translational capacity of amino acid analogs has technical limitations. Therefore, a rapid and reliable  in silico  test for N AA  recognition by AARS would be advantageous in experimental design. We chose tryptophanyl-tRNA synthetase from  Escherichia coli  as a model system for docking studies with various tryptophan analogs using the FlexX-Pharm strategy. We were able to calculate relative binding energies for Trp analogs in TrpRS that correlate well with their translational activities in  E. coli . In particular, FlexX-Pharm predicted the binding sites of fluoro-, amino-, hydroxyl- and aza-containing Trp analogs within 1.5 Å of Trp in the homology model of  E. coli  TrpRS. Therefore, the use of ligand docking prior to N AA  incorporation experiments might provide a straightforward means for determining N AA  that can be efficiently incorporated into a protein.

Docking of tryptophan analogs to trytophanyl-tRNA synthetase: implications for non-canonical amino acid incorporations