Tryptophan absorbs at a maximum wavelength of 280 nm. In a cuvette (1 cm-optical path length), a 200 µM tryptophan solution shows an absorbance value at 280 nm of 1.2. 1- Calculate & the molar absorption coefficient (also called molar extinction coefficient) of tryptophan. A solution of protein X, at the concentration of 25 µM, shows an absorbance value at 280 nm of 0.6. The protein X has no tyrosine and no phenylalanine residues. 2- Determine the number of tryptophan residues of the protein X.

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Tryptophan absorbs at a maximum wavelength of 280 nm. In a cuvette (1 cm-optical
path length), a 200 µM tryptophan solution shows an absorbance value at 280 nm of
1.2.
1- Calculate & the molar absorption coefficient (also called molar extinction
coefficient) of tryptophan.
A solution of protein X, at the concentration of 25 µM, shows an absorbance value at
280 nm of 0.6. The protein X has no tyrosine and no phenylalanine residues.
2- Determine the number of tryptophan residues of the protein X.
Transcribed Image Text:Tryptophan absorbs at a maximum wavelength of 280 nm. In a cuvette (1 cm-optical path length), a 200 µM tryptophan solution shows an absorbance value at 280 nm of 1.2. 1- Calculate & the molar absorption coefficient (also called molar extinction coefficient) of tryptophan. A solution of protein X, at the concentration of 25 µM, shows an absorbance value at 280 nm of 0.6. The protein X has no tyrosine and no phenylalanine residues. 2- Determine the number of tryptophan residues of the protein X.
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