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Chapter 5: Q5-7P (page 127)

(a) In what order would the amino acids Arg, His, and Leu be eluted from a carboxymethyl column at pH6 ?

(b) In what order would Glu, Lys, and Val be eluted from a diethylaminoethyl column at pH 8?

Short Answer

Expert verified

a) In the following order Leu, His, Arg would the amino acids Arg, His, and Leu be eluted from a carboxymethyl column at pH 6.

b) In the following order Lys, Val, Glu would Glu, Lys, and Val be eluted from a diethylaminoethyl column at pH 8.

Step by step solution

01

Definition of amino acids

The building blocks of proteins are amino acids, which are the chemical compounds that come together to make proteins. These biomolecules are essential for human growth and development and are engaged in a number of biological and chemical processes in the body.

02

Find the correct order to be eluted from a carboxymethyl column at pH6.

a) Elution is the process of extracting one material from another using a solvent. Larger and non-polar molecules are the first to elute.

The amino acids Arg, His, and Leu would be eluted from a carboxymethyl column at pH6 in the following order: Leu, His, Arg.

03

Find the correct order to elute from a diethylaminoethyl column at pH8.

b) Elution is the process of extracting one material from another using a solvent. Larger and non-polar molecules are the first to elute.

Glu, Lys, and Val would be eluted from a diethylaminoethyl column at pH8 in the following order: Lys, Val, Glu.

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Most popular questions from this chapter

Separate cleavage reactions of a polypeptide by CNBr and chymotrypsin yield fragments with the following amino acid sequences. What is the sequence of the intact polypeptide?

CNBr treatment

1. Arg鈥揂la鈥揟yr鈥揋ly鈥揂sn

2. Leu鈥揚he鈥揗et

3. Asp鈥揗et

Chymotrypsin

4. Met鈥揂rg鈥揂la鈥揟yr

5. Asp鈥揗et鈥揕eu鈥揚he

6. Gly鈥揂sn

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?

You are trying to purify a protein that is soluble in a solution of 2 M ammonium sulfate. After centrifugation to remove other proteins that have precipitated at this high salt concentration, you recover the supernatant to assay the target protein鈥檚 activity in a cell culture system.

(a) Explain why the cells die when incubated with the supernatant.

(b) What procedure could you perform to correct the problem? (Hint: See Section 2-1D).

Question: Purification tables are often used to keep track of the yield and purification of a protein. The specific activity is a ratio of the amount of the protein of interest, in this case Mb, obtained at a given step (渭mol or enzyme units) divided by the amount (mg) of total protein. The yield is the ratio of the amount of the protein of interest obtained at a given step (渭mol or enzyme units) divided by the original amount present in the crude extract, often converted to percent yield by multiplying by 100. The fold purification is the ratio of the specific activity of the purified protein to that of the crude preparation.

(a) For the purification table below, calculate the specific activity, % yield, and fold purification for the empty cells.

(b) Which step鈥擠EAE or affinity chromatography鈥攃auses the greatest loss of Mb?

(c) Which step causes the greater purification of Mb?

(d) If you wanted to use only one purification step, which technique would you choose?

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.
See all solutions

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