Organic Chemistry
8th Edition
ISBN: 9781305580350
Author: William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher: Cengage Learning
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Question
Chapter 27.2, Problem 27.3P
Interpretation Introduction
Interpretation:
The behaviour of a mixture of glutamic acid, arginine and valine on paper electrophoresis at
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Chapter 27 Solutions
Organic Chemistry
Ch. 27.1 - Of the 20 protein-derived amino acids shown in...Ch. 27.2 - Prob. 27.2PCh. 27.2 - Prob. 27.3PCh. 27.3 - Draw a structural formula for Lys-Phe-Ala. Label...Ch. 27.4 - Which of these tripeptides are hydrolyzed by...Ch. 27.4 - Deduce the amino acid sequence of an undecapeptide...Ch. 27.6 - Prob. 27.7PCh. 27 - What amino acid does each abbreviation stand for?...Ch. 27 - The configuration of the chiral center in -amino...Ch. 27 - Assign an R or S configuration to the chiral...
Ch. 27 - Prob. 27.11PCh. 27 - Prob. 27.12PCh. 27 - Draw zwitterion forms of these amino acids. (a)...Ch. 27 - Prob. 27.14PCh. 27 - Why is Arg often referred to as a basic amino...Ch. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Both norepinephrine and epinephrine are...Ch. 27 - Prob. 27.22PCh. 27 - Draw a structural formula for the form of each...Ch. 27 - Prob. 27.24PCh. 27 - Write the zwitterion form of alanine and show its...Ch. 27 - Prob. 27.26PCh. 27 - Write the form of aspartic acid most prevalent at...Ch. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - For lysine and arginine, the isoelectric point,...Ch. 27 - Prob. 27.31PCh. 27 - Account for the fact that the isoelectric point of...Ch. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - At pH 7.4, the pH of blood plasma, do the majority...Ch. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - A chemically modified guanidino group is present...Ch. 27 - Draw a structural formula for the product formed...Ch. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - A decapeptide has the following amino acid...Ch. 27 - Following is the primary structure of glucagon, a...Ch. 27 - Prob. 27.45PCh. 27 - Draw a structural formula of these tripeptides....Ch. 27 - Estimate the pI of each tripeptide in Problem...Ch. 27 - Glutathione (G-SH), one of the most common...Ch. 27 - Following are a structural formula and a...Ch. 27 - Prob. 27.50PCh. 27 - Prob. 27.51PCh. 27 - Prob. 27.52PCh. 27 - Prob. 27.53PCh. 27 - Prob. 27.54PCh. 27 - Distinguish between intermolecular and...Ch. 27 - Prob. 27.56PCh. 27 - Prob. 27.57P
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Similar questions
- 1arrow_forwardWhich amino acid would migrate the furthest toward the NEGATIVE electrode, during paper electrophoresis at pH 7.0? glutamtic acid glycine glutamine arginine. alaninearrow_forwardRank the migration rate of the following amino acids in ascending order towards the cathode when separated by electrophoresis in a solution of pH = 7. I. Lysine: pI = 9.87, II. Aspartate: pI = 5. 95, III. Alanine: pI = 6.02arrow_forward
- How does the shape of a titration curve confirm the fact that the pH region of greatest buffering power for an amino acid solution is around its pK's? Name four factors (bonds or other forces) that contribute to stabilizing the native structure of a protein, and describe one condition or reagent that interferes with each type of stabilizing force. Why is silk fibroin so strong, but at the same time so soft and flexible?arrow_forwardUse the following chromatogram of standard amino acids: Which of the following statements BEST describe the given chromatogram? Peaks 14, 18, 20 and 22 have the lowest concentrations and highest affinity to the mobile phase. The peaks are narrow and show clear separation of the mixture. Peaks 4, 5, 11 and 24 have the highest concentrations in the mixture and highest affinity to the mobile phase. The peaks are narrow and show suboptimal conditions for separation.arrow_forwardAbout a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.arrow_forward
- A student analyzed a mixture of amino acids using thin layer chromatography where the stationary phase is a silica-coated plate. For the mobile phase, he used 50% ethyl acetate in hexane. The mixture contained three (3) amino acids whose structures are shown below. OH Hollo HO OH OH OH NH₂ NH₂ NH₂ Threonine Valine Glutamic acid a. Identify spots A, B, and C in the developed TLC plate below based on the structures of the amino acids above (ie. which spot is threonine, valine, glutamic acid?). Hint: determine how the structures of the given amino acids differ A. BO С. b. Threonine can be phosphorylated using an enzyme called protein kinase. Given the same conditions the student used in his analysis, will the phosphorylated threonine have a higher, smaller, or the same Rf value compared to threonine? Which of the following compounds would have the lowest Rf value in a TLC analysis? A. Hexane-2,3-diol B. Benzene C. Diethyl ether D. 1,3,5-cyclohexanetriolarrow_forwardPlot the titration curves of valine and lysine amino acids in basic medium and calculate the pI values. valine (pKa1: 2,32; pKa2: 9,62) lysine (pKa1: 2,18; pKa2: 8,95; pKa3:10,53)arrow_forwardA mixture of valine, glycine, isoleucine, aspartic acid, phenylalanine, arginine, lysine, asparagine, and methionine are put into an electrophoresis apparatus, with the buffer pH=6.5pH=6.5. Sort each amino acid according to its charge in the buffer with a pHpH of 6.5.arrow_forward
- 3arrow_forwardBiuret Assay accurately quantify protein concentration within the range of 5-150 mg/mL. JUSTIFY THE STATEMENT.arrow_forwardA mixture of seven amino acids (glycine, glutamate, leucine, lysine, alanine, isoleucine, and aspartate) is separated by chromatography. Explain why only six spots show up when the chromatographic plate is coated with ninhydrin and heated.arrow_forward
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