Transfer RNAs (tRNA) are short RNA molecules (76 nucleotides) that deliver amino acids to the ribosome, where they join to a growing peptide chain during protein synthesis. Transfer RNAs fold into 3-D structures, stabilized by hydrogen bonding between complementary bases. Individual amino acids are joined to the 3’-end of the tRNA. On the other side of the molecule is the anticodon. This is the portion of the tRNA that recognizes the triplet codons on the messenger RNA (mRNA). In 1964, Robert Holley isolated and determined the structure of tRNA. Just 4 years later, he was awarded the 1968 Nobel Prize in Physiology or Medicine, a prize he shared with H. Gobind Khorana and Marshall Nirenberg; all 3 greatly contributed to the areas of transcription and translation.
In the plaster 3-D model, the tRNA protein is shown in spacefill format. The phosphate backbone of the tRNA is white, the 4 bases are red, the anticodon is blue, and the 3’-end (where the amino acid is bound) is yellow. The white, nylon, alpha carbon backbone model shows additional details not seen on the plaster model.
To date 31 researchers have been awarded Nobel Prizes for their investigations of RNA, spanning 50 years from 1959 to 2009.
The Molecule of the Month by scientist, author and artist Dr. David Goodsell includes an introduction to the structure and function of the chosen molecule and a discussion of its relevance to human health and welfare. Molecule of the Month articles are frequently referred to by teachers, students and researchers. More...