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The complete data for Tryptophan ... Molar mass: 204.23 g·mol −1 Systematic name: (S)-2-Amino-3-(1H-indol-3-yl)-propanoic acid Abbreviations: W, Trp Synonyms:
In biochemistry, the molar absorption coefficient of a protein at 280 nm depends almost exclusively on the number of aromatic residues, particularly tryptophan, and can be predicted from the sequence of amino acids. [6] Similarly, the molar absorption coefficient of nucleic acids at 260 nm can be predicted given the nucleotide sequence.
[1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and tryptophan. Of the aromatic amino acids, tryptophan has the highest extinction coefficient; its absorption maximum occurs at 280 nm. The absorption maximum of tyrosine occurs at 274 nm. [3]
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.
Extinction coefficient refers to several different measures of the absorption of light in a medium: Attenuation coefficient , sometimes called "extinction coefficient" in meteorology or climatology Mass extinction coefficient , how strongly a substance absorbs light at a given wavelength, per mass density
An example is the determination of bilirubin in blood plasma samples. The spectrum of pure bilirubin is known, so the molar attenuation coefficient ε is known. Measurements of decadic attenuation coefficient μ 10 are made at one wavelength λ that is nearly unique for bilirubin and at a second wavelength in order to correct for possible ...
The molar extinction coefficient of Hb has its highest absorption peak at 420 nm and a second peak at 580 nm. Its spectrum then gradually decreases as light wavelength increases. On the other hand, H b O 2 {\displaystyle HbO2} shows its highest absorption peak at 410 nm, and two secondary peaks at 550 nm and 600 nm.
Tryptophan 2,3-dioxygenase plays a central role in the physiological regulation of tryptophan flux in the human body, as part of the overall biological process of tryptophan metabolism. TDO catalyses the first and rate-limiting step of tryptophan degradation along the kynurenine pathway and thereby regulates systemic tryptophan levels. [5]