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Download QR code; Print/export ... The complete data for Tryptophan ... Structure. Crystal data: Spectral data. UV-Vis: IR: NMR: MS
Tryptophan ball and stick model spinning. Tryptophan (symbol Trp or W) [3] is an α-amino acid that is used in the biosynthesis of proteins.Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent.
Three sequences, UAG, UGA, and UAA, known as stop codons, [note 1] do not code for an amino acid but instead signal the release of the nascent polypeptide from the ribosome. [7] In the standard code, the sequence AUG—read as methionine—can serve as a start codon and, along with sequences such as an initiation factor, initiates translation.
Structure of the trp operon. The trp operon is a group of genes that are transcribed together, encoding the enzymes that produce the amino acid tryptophan in bacteria. The trp operon was first characterized in Escherichia coli, and it has since been discovered in many other bacteria. [1]
Efforts to understand how proteins are encoded began after DNA's structure was discovered in 1953. The key discoverers, English biophysicist Francis Crick and American biologist James Watson, working together at the Cavendish Laboratory of the University of Cambridge, hypothesied that information flows from DNA and that there is a link between DNA and proteins. [2]
The Tryptophan operon leader is an RNA element found at the 5′ of some bacterial tryptophan operons. The leader sequence can form two different structures known as the terminator and the anti-terminator, based on the Tryptophan amounts in the cell. The leader also codes for very short peptide sequence that is rich in tryptophan.
Leucine is an example of a typical amino acid. Idiosyncratic amino acids - there are few similar amino acids that they can mutate to through single nucleotide substitution. In this case most amino acid replacements will be disruptive for protein function. Tryptophan is an example of an idiosyncratic amino acid. [8]
Tryptophan synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyzes the final two steps in the biosynthesis of tryptophan. [1] [2] It is commonly found in Eubacteria, [3] Archaebacteria, [4] Protista, [5] Fungi, [6] and Plantae. [7] However, it is absent from Animalia. [8] It is typically found as an α2β2 tetramer.