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zheka24 [161]
3 years ago
4

If we have a protein that has a molar extinction coefficient of 17900 M-1cm-1 at 280nm.

Biology
1 answer:
TiliK225 [7]3 years ago
5 0

Answer:

a) In this protein, there are 3 Tryptophan residues

b) c = 3.128 x 10^-5 M

Explanation:

Molar extinction coefficient (ε) tells us how strongly some chemical substance can absorb light at particular wavelength. In proteins, aromatic amino acids such as Tyrosine and Tryptophan are capable of absorbing the light at 280 nm.

a) ε (protein) = 17900 M-1cm-1

We know that protein has one Tyr, which ε equals 1400 M-1cm-1

If we deduct this value from total ε of protein we wil get ε that comes from all Trp in protein.

ε (Trp) = ε (protein) - ε (Tyr)

ε (Trp) = 17900 M-1cm-1 - 1400 M-1cm-1

ε (Trp) = 16500 M-1cm-1

Then, to get the exact numbers od Trp in protein, we divide this ε with known ε of Trp which is 5500 M-1cm-1

number of Trp: 16500 / 5500 = 3

In this protein, there are 3 Tryptophan residues.

b) The equation which connects all this values is:

                                      A = εlc

A is the amount of light absorbed by the sample for a particular wavelength

ε is the molar extinction coefficient

l is the distance that the light travels through the solution

c is the concentration of the absorbing species per unit volume

A = 0.56

ε = 17900 M-1cm-1

l = 1cm

c = ?

c = A/(εxl)

c = 0.56/(17900 M-1cm-1 x 1cm)

c = 3.128 x 10^-5 M

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