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The molar absorptivity of a tyrosine residue at 280 nm is 2000 M-1cm-1, while for tryptophan it is 5500 M-1cm-1. A protein has been isolated that is known to contain one tyrosine residue and an unknown number of tryptophans. A 1.0 micromolar solution of this protein is placed in a 1.0 cm cuvette and the absorbance at 280 nm is measured as 0.024. How many tryptophans are in the protein

User Ctx
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Answer:

There are 4 tryptophans in the protein.

Step-by-step explanation:

According to question, protein contains one tyrosine residue and say x number of tryptophans.

Concentration of protein solution = 1.0 micromolar =
1.0* 10^(-6) Molar

Molar absorptivity of a protein solution :
\epsilon


\epsilon = \epsilon _(tyro)+\epsilon _(tryp)


=1* 2000 M^(-1)cm^(-1)+x* 5500 M^(-1)cm^(-1)

Length of the cuvette = l = 1.0 cm

Absorbance of protein solution at 280 nm = A = 0.024


A=\epsilon * l* c ( Beer-Lambert's law)


0.024=(1* 2000 M^(-1)cm^(-1)+x* 5500 M^(-1)cm^(-1))* 1 cm* 1.0* 10^(-6) M

Solving for x :

x = 4

There are 4 tryptophans in the protein.

User Raleigh Buckner
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