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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.
The complete data for Tryptophan ... C 11 H 12 N 2 O 2 Molar mass: 204.23 g·mol −1 Systematic name: (S)-2-Amino-3-(1H-indol-3-yl) ... Gas properties. Hazard ...
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.
[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]
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.
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 ...
Using Bradford can be advantageous against these molecules because they are compatible to each other and will not interfere. [ 16 ] The linear graph acquired from the assay (absorbance versus protein concentration in μg/mL) can be easily extrapolated to determine the concentration of proteins by using the slope of the line.