MODIFIED MASTERING CHEMISTRY W/ ETEXT
8th Edition
ISBN: 9781323782507
Author: Bruice
Publisher: PEARSON
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Chapter 21.3, Problem 5P
Interpretation Introduction
Interpretation:
Concept Introduction:
Acid-base properties of Amino acids:
Every amino acid has a carbonyl group and an amino group, and each group can exist in an acidic form or a basic form, depending on
The compound exists primarily in the acidic form in solutions that are more acidic than their
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Chapter 21 Solutions
MODIFIED MASTERING CHEMISTRY W/ ETEXT
Ch. 21.1 - a. Explain why, when the imidazole ring of...Ch. 21.2 - a. Which isomer(R)-alanine or (S)-alanineis...Ch. 21.2 - Prob. 4PCh. 21.3 - Prob. 5PCh. 21.3 - Prob. 6PCh. 21.3 - Draw the predominant form for glutamate in a...Ch. 21.3 - a. Why is the pKa of the glutamate side chain...Ch. 21.4 - Calculate the pI of each of the following amino...Ch. 21.4 - a. Which amino acid has the lowest pI value? b....Ch. 21.4 - Prob. 12P
Ch. 21.4 - Prob. 13PCh. 21.4 - Explain why the pI of lysine is the average of the...Ch. 21.5 - What aldehyde is formed when valine is treated...Ch. 21.5 - Prob. 16PCh. 21.5 - Prob. 17PCh. 21.5 - Prob. 18PCh. 21.5 - Prob. 19PCh. 21.6 - Why is excess ammonia used in the preceding...Ch. 21.6 - Prob. 21PCh. 21.6 - What amino acid is formed using the...Ch. 21.6 - Prob. 23PCh. 21.6 - What amino acid is formed when the aldehyde used...Ch. 21.7 - Esterase is an enzyme that catalyzes the...Ch. 21.8 - Draw the tetrapeptide Ala-Thr-Asp-Asn and indicate...Ch. 21.8 - Draw the resonance contributors of the peptide...Ch. 21.8 - Which bonds in the backbone of a peptide can...Ch. 21.9 - An opioid pentapeptide has the following...Ch. 21.9 - What is the configuration about each of the...Ch. 21.9 - Glutathione is a tripeptide whose function is to...Ch. 21.10 - What dipeptides would be formed by heating a...Ch. 21.10 - Suppose you are trying to synthesize the dipeptide...Ch. 21.10 - Show the steps in the synthesis of the...Ch. 21.10 - a. Calculate the overall yield of bradykinin when...Ch. 21.11 - Show the steps in the synthesis of the...Ch. 21.13 - Prob. 37PCh. 21.13 - In determining the primary structure of insulin,...Ch. 21.13 - A decapeptide undergoes partial hydrolysis to give...Ch. 21.13 - Explain why cyanogen bromide does not cleave on...Ch. 21.13 - Indicate the peptides produced from cleavage by...Ch. 21.14 - Prob. 43PCh. 21.14 - Three peptides were obtained from a trypsin...Ch. 21.14 - Prob. 45PCh. 21.15 - How would a protein that resides in the nonpolar...Ch. 21.16 - a. Which would have the greatest percentage of...Ch. 21.17 - When apples that have been cut are exposed to...Ch. 21 - Glycine has pK2 values of 2.34 and 9.60. At what...Ch. 21 - Prob. 50PCh. 21 - A titration curve is a plot of the pH of a...Ch. 21 - Prob. 52PCh. 21 - Aspartame (its structure is on page 1007) has a pl...Ch. 21 - Draw the form of aspartate that predominates at...Ch. 21 - Show how phenylalanine can be prepared by...Ch. 21 - A professor was preparing a manuscript for...Ch. 21 - What aldehydes are formed when the following amino...Ch. 21 - Prob. 58PCh. 21 - Determine the amino acid sequence of a polypeptide...Ch. 21 - Prob. 60PCh. 21 - Prob. 61PCh. 21 - Which is the more effective buffer at...Ch. 21 - Identify the location and type of charge on the...Ch. 21 - Draw the product obtained when a lysine side chain...Ch. 21 - After the polypeptide shown below was treated with...Ch. 21 - Treatment of a polypeptide with 2-mercaptoethanol...Ch. 21 - Show how aspartame can be synthesized using DCCD.Ch. 21 - -Amino acids can be prepared by treating an...Ch. 21 - Reaction of a polypeptide with carboxypeptidase A...Ch. 21 - a. How many different octapeptides can be made...Ch. 21 - Glycine has pKa values of 2.3 and 9.6. Do you...Ch. 21 - A mixture of 15 amino acids gave the fingerprint...Ch. 21 - Write the mechanism for the reaction of an amino...Ch. 21 - Prob. 74PCh. 21 - Show how valine can be prepared by a. a...Ch. 21 - The primary structure of -endorphin, a peptide...Ch. 21 - A chemist wanted to test his hypothesis that the...Ch. 21 - Propose a mechanism for the rearrangement of the...Ch. 21 - A normal polypeptide and a mutant of the...Ch. 21 - Determine the amino acid sequence of a polypeptide...
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- A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)arrow_forwardThe peptide structure attached below is most likely a? P.S. Both images are the same.arrow_forwardThere are two pH values in which Glutamic acid will have an a complete net charge of 2.17? what is the lowest PH1 and highest of pH2 round your amswers to the nearest 0.1 no orher information was providedarrow_forward
- a) A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of the solution was 2.8. Describe the state of the functional groups of the amino acid at the initial pH and at 10.5.b) Briefly explain how you will separate amino acids mixture using the charge difference between the amino acids. c) A given glycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that pKa1 and pKa2 of glycine are 2.34 and 9.60, respectively. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid, if [x] and [y] are the concentrations of dissociated and undissociated amino acid, respectively.arrow_forwardDraw the tetrapeptide represented by HLQS at physiological pH (pH=7.4), Include proper stereochemistryarrow_forwardA compound is known to have a free amino group with a pKa of 8.6, and one other ionizible group with a pKa between 5 and 7. To 90mL of a 0.150M solution of this compound at pH 7.80 was added 35 mL of a solution of 0.18 M HCl. The pH changed to 6.40. What is the pKa of the second ionizable group?arrow_forward
- Give typed solution only Which of the amino acids shown represents the structure of Ile at pH 10?arrow_forwardPlease help me with the following 1) sketch a phosphodiester bond 2) Make the two amino from the image below. And contrast the polarity of the side chainsarrow_forwardGlutamic acid is a naturally occurring α-amino acid that contains acarboxy group in its R group side chain. (Glutamic acid isdrawn in its neutral form with no charged atoms, a form that does not actually exist at any pH.) a.) What form of glutamic acid exists at pH = 1?b.) If the pH is gradually increased, what form of glutamic acid exists afterone equivalent of base is added? After two equivalents? After threeequivalents?c.) Propose a structure of monosodium glutamate, the common flavorenhancer known as MSG.arrow_forward
- Valine has pKa's of 2.286 and 9.719. Estimate the fractional composition of Valine in the -1 form at pH=6.arrow_forwardThis is a homework question... In nature, amino acids in proteins are typically found in the L-configuration. This is basedon it’s relationship to D- and L-glyceraldehyde. Shown below is the structure of the amino acidasparagine (Asn) at physiological pH. As written does histidine have an L(S)- or D(R)-configuration? Be sure to show how you derived your answer:arrow_forwardA protein has a number of aspartyl and gluatmyl residues, what would be the expected pI for this protein? a. Basic pI b. Neutral pI c. Cannot be determined d. Acidic pIarrow_forward
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