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Chapter 5: Q4P (page 127)

Protein X has an absorptivity of 0.4mL 路 mg-1路 cm-1 at 280nm. What is the absorbance at 280nm of a 2.0 mg 路 mL-1solution of protein X? (Assume the light path is 1cm.)

Short Answer

Expert verified

The absorbance at 280 nm of a 2.0 mg 路 mL鈥�1 solution of protein X is 0.8.

Step by step solution

01

Definition of protein

Proteins are huge molecules made up of fundamental building blocks called amino acids.

02

Find the absorbance of protein X

According to Beer-Law, Lambert's A =鈭�CL, where A is the absorbance of the solute. The absorptivity is;

The solute concentration is C, and the length of the light path is I in cm.

Use the formula:

A=鈭�CI

Substitute the values:

A = (0.4mLmg-1CM-1)(2.0mgmL-1)(1cm)

A = 0.8

Therefore, the total absorbance is 0.8.

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Most popular questions from this chapter

Consult Table 5-1 to complete the following: (a) On a plot of absorbance at 280 nm versus elution volume, sketch the results of gel filtration of a mixture containing human cytochrome c and bacteriophage T7 RNA polymerase and identify each peak. (b) Sketch the results of SDS-PAGE of the same protein mixture showing the direction of migration and identifying each band.

Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides:

1. Ala鈥揤al鈥揅ys鈥揂rg鈥揟hr鈥揋ly鈥揅ys鈥揕ys鈥揂sn鈥揚he鈥揕eu

2. Tyr鈥揕ys鈥揅ys鈥揚he鈥揂rg鈥揌is鈥揟hr鈥揕ys鈥揅ys鈥揝er

Treatment of the intact polypeptide with trypsin yields fragments with the following amino acid compositions:

3. (Ala, Arg, Cys2, Ser, Val)

4. (Arg, Cys2, Gly, Lys, Thr, Phe)

5. (Asn, Leu, Phe)

6. (His, Lys, Thr)

7. (Lys, Tyr)

Indicate the positions of the disulfide bonds in the intact polypeptide.

You wish to determine the sequence of a polypeptide that has the following amino acid composition.

1 Ala 4 Arg 2 Asn 3 Asp 4 Cys 3 Gly 1 Gln 4 Glu 1 His 1 Lys 1 Met 1 Phe 2 Pro 4 Ser 2 Tyr 1 Trp

(a) What is the maximum number of peptides you can expect if you cleave the polypeptide with cyanogen bromide?

(b) What is the maximum number of peptides you can expect if you cleave the polypeptide with chymotrypsin?

(c) Analysis of the intact polypeptide reveals that there are no free sulfhydryl groups. How many disulfide bonds are likely to be present?

(d) How many different arrangements of disulfide bonds are possible?

What types of information can be retrieved from a protein sequence database?

(a) The ESI-MS spectrum below was obtained for hen egg-white lysozyme (HEWL). Using peaks 5 and 6, calculate the molecular mass of HEWL (see Sample Calculation 5-1).

[http://www.astbury.leeds.ac.uk/facil/MStut/mstutorial.htm. Published by A.E. Ashcroft, Astbury Centre for Structural Molecular Biology, University of Leeds (2000)]

(b) What is the charge on the ion that makes peak 5?
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