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Transfer RNA (abbreviated tRNA) is a small RNA chain (74-93 nucleotides) that transfers a specific amino acid to a growing polypeptide chain at the ribosomal site of protein synthesis during translation. It has sites for amino-acid attachment and codon (a particular sequence of 3 bases) recognition. The codon recognition is different for each tRNA and is determined by the anticodon region, which contains the complementary bases to the ones encountered on the mRNA. Each tRNA molecule binds only one type of amino acid, but because the genetic code is degenerate, more than one codon exists for each amino acid. Transfer RNA is the "adaptor" molecule hypothesized by Francis Crick, which mediates recognition of the codon sequence in mRNA and allows its translation into the appropriate amino acid.
Structure of tRNAtRNA has primary structure (the order of nucleotides from 5' to 3'), secondary structure (usually visualized as the cloverleaf structure), and tertiary structure (all tRNAs have a similar L-shaped 3D structure that allows them to fit into the P and A sites of the ribosome). Features
AminoacylationAminoacylation is the process of adding an aminoacyl group to a compound. Each tRNA is aminoacylated (or charged) with a specific amino acid by an aminoacyl tRNA synthetase. There is often just one aminoacyl tRNA synthetase for each amino acid, despite the fact that there can be more than one tRNA, and more than one anticodon, for an amino acid. Recognition of the approriate tRNA by the synthetases in not mediated solely by the anticodon, and the acceptor stem often plays a prominent role. Reaction:
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