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Describe the behavior of a mixture of glutamic acid, arginine, and valine on paper electrophoresis at \(\mathrm{pH} 6.0\).

Short Answer

Expert verified
Answer: At pH 6.0, glutamic acid will have a negative charge and will move towards the anode (positive electrode), arginine will have a positive charge and will move towards the cathode (negative electrode), and valine will have a neutral charge, resulting in minimal or no movement during the electrophoresis process.

Step by step solution

01

Understanding paper electrophoresis

Paper electrophoresis is a technique used to separate biological molecules, such as amino acids, based on their charge and size. In this technique, a mixture of molecules is placed on a paper strip that is moistened with a buffer solution, and then an electric field is applied across the paper. Molecules with different charges will move towards the opposite electrode, and their mobility depends on their size and charge.
02

Determining the properties of glutamic acid, arginine, and valine

To understand the behavior of glutamic acid, arginine, and valine on paper electrophoresis, we need to know their properties, particularly their isoelectric points (pI) -- the pH at which the amino acid has no net charge. - Glutamic acid: An acidic amino acid with a carboxyl side chain. It has pI = 3.22. - Arginine: A basic amino acid with a guanidino side chain. It has pI = 10.76. - Valine: A nonpolar, aliphatic amino acid with no charged side chain. It has pI = 6.00.
03

Determining the charge of each amino acid at pH 6.0

At any given pH, the charge of an amino acid can be positive, negative, or neutral. We will determine the charge of each amino acid at pH 6.0: - Glutamic acid (pI = 3.22): Since pH 6.0 > pI, glutamic acid will have a negative charge at pH 6.0. - Arginine (pI = 10.76): Since pH 6.0 < pI, arginine will have a positive charge at pH 6.0. - Valine (pI = 6.00): Since pH 6.0 = pI, valine will have a neutral charge at pH 6.0.
04

Predicting the movement of amino acids on paper electrophoresis

Now that we know the charge of each amino acid at pH 6.0, we can predict how they will move in the electric field during electrophoresis: - Glutamic acid (negatively charged): It will move towards the anode (the positive electrode). - Arginine (positively charged): It will move towards the cathode (the negative electrode). - Valine (neutral charge): It will not move or will have minimal mobility since it has no net charge to be attracted to either electrode. As a result, the mixture of these three amino acids will show three distinct bands on the paper electrophoresis strip, each representing the location of the amino acid based on its charge and mobility at pH 6.0.

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Most popular questions from this chapter

How many different tetrapeptides can be made under the following conditions? (a) The tetrapeptide contains one unit each of Asp, Glu, Pro, and Phe. (b) All 20 amino acids can be used, but each only once.

Following is the primary structure of glucagon, a polypeptide hormone of 29 amino acids. Glucagon is produced in the \(\alpha\)-cells of the pancreas and helps maintain blood glucose levels in a normal concentration range. Which peptide bonds are hydrolyzed when this polypeptide is treated with each reagent? (a) Phenyl isothiocyanate (b) Chymotrypsin (c) Trypsin (d) \(\mathrm{BrCN}\)

Dinitrofluorobenzene, very often known as Sanger's reagent after the English chemist Frederick Sanger who popularized its use, reacts selectively with the \(N\)-terminal amino group of a polypeptide chain. Sanger was awarded the 1958 Nobel Prize in Chemistry for his work in determining the primary structure of bovine insulin. One of the few people to be awarded two Nobel Prizes, he also shared the 1980 award in chemistry with American chemists Paul Berg and Walter Gilbert for the development of chemical and biological analyses of DNA. Following reaction with 2,4 -dinitrofluorobenzene, all amide bonds of the polypeptide chain are hydrolyzed and the amino acid labeled with a 2,4-dinitrophenyl group is separated by either paper or column chromatography and identified. (a) Write a structural formula for the product formed by treatment of the \(N\)-terminal amino group with Sanger's reagent and propose a mechanism for its formation. (b) When bovine insulin is treated with Sanger's reagent followed by hydrolysis of all peptide bonds, two labeled amino acids are detected: glycine and phenylalanine. What conclusions can be drawn from this information about the primary structure of bovine insulin? (c) Compare and contrast the structural information that can be obtained from use of Sanger's reagent with that from use of the Edman degradation.

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