Introduction To General, Organic, And Biochemistry
12th Edition
ISBN: 9781337571357
Author: Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher: Cengage Learning
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Textbook Question
Chapter 21.3, Problem 21.3QC
What is the overall charge
(a) Isoleucine
(b) Arginine
(c) Aspartic acid
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Calculate the pH at which the e-amino group of lysine is 25% dissociated.
Which amino acid has the greatest amount of negative charge at pH = 6.20?
For aspartic and glutamic acids, the isoelectric point occurs at a pH where the net charge on the two carboxyl groups is -1 and balances the charge of +1 on the a-amino group. Calculate pI for these amino acids.
Chapter 21 Solutions
Introduction To General, Organic, And Biochemistry
Ch. 21.1 - Prob. 21.1QCCh. 21.2 - Prob. 21.2QCCh. 21.3 - What is the overall charge (+,0, or ) for the...Ch. 21.4 - Problem 22-1 Show how to form the dipeptide...Ch. 21.5 - Prob. 21.5QCCh. 21.7 - Prob. 21.6QCCh. 21.8 - Prob. 21.7QCCh. 21.8 - Prob. 21.8QCCh. 21.10 - Prob. 21.9QCCh. 21 - 22-5 What are the functions of (a) ovalbumin and...
Ch. 21 - 22-6 The members of which class of proteins are...Ch. 21 - 22-7 What is the function of an immunoglobulin?Ch. 21 - Prob. 4PCh. 21 - 22-9 What is the difference in structure between...Ch. 21 - 22-10 Classify the following amino acids as...Ch. 21 - 22-11 Which amino acid has the highest percentage...Ch. 21 - Prob. 8PCh. 21 - Prob. 9PCh. 21 - Prob. 10PCh. 21 - Prob. 11PCh. 21 - Prob. 12PCh. 21 - 22-17 What are the similarities and differences in...Ch. 21 - 22-18 Draw the structures of L- and D-valine.Ch. 21 - Prob. 15PCh. 21 - 22-20 Show how alanine, in solution at its...Ch. 21 - 22-21 Explain why an amino acid cannot exist in an...Ch. 21 - 22-22 Draw the structure of valine at pH 1 and at...Ch. 21 - Prob. 19PCh. 21 - 22-24 Draw the most predominant form of histidine...Ch. 21 - 22-25 Draw the most predominant form of lysine at...Ch. 21 - Prob. 22PCh. 21 - 22-27 Show by chemical equations how alanine and...Ch. 21 - 22-28 A tetrapeptide is abbreviated as DPKH. Which...Ch. 21 - 22-29 Draw the structure of a tripeptide made of...Ch. 21 - 22-30 (a) Use the three-letter abbreviations to...Ch. 21 - 22-31 A polypeptide chain is made of alternating...Ch. 21 - Prob. 28PCh. 21 - 22-33 Which of the three functional groups on...Ch. 21 - Prob. 30PCh. 21 - 22-35 Why is histidine considered a basic amino...Ch. 21 - Prob. 32PCh. 21 - Prob. 33PCh. 21 - 22-38 Why does proline not absorb light at 280 nm?Ch. 21 - Prob. 35PCh. 21 - Prob. 36PCh. 21 - Prob. 37PCh. 21 - 22-42 (a) How many atoms of the peptide bond lie...Ch. 21 - 22-43 (a) Draw the structural formula of the...Ch. 21 - 22-44 How can a protein act as a buffer?Ch. 21 - 22-45 Proteins are least soluble at their...Ch. 21 - 22-46 How many different tripeptides can be made...Ch. 21 - 22-47 How many different tetrapeptides can be made...Ch. 21 - 22-48 How many amino acid residues in the A chain...Ch. 21 - 22-49 Based on your knowledge of the chemical...Ch. 21 - Prob. 46PCh. 21 - 22-59 What is the effect of salt bridges on the...Ch. 21 - Prob. 48PCh. 21 - 22-61 Polyglutamic acid (a polypeptide chain made...Ch. 21 - 22-62 Distinguish between intermolecular and...Ch. 21 - 22-63 Identify the primary, secondary, and...Ch. 21 - 22-64 If both cysteine residues on the B chain of...Ch. 21 - 22-65 (a) What is the difference in the quaternary...Ch. 21 - Prob. 54PCh. 21 - Prob. 55PCh. 21 - Prob. 56PCh. 21 - Prob. 57PCh. 21 - Prob. 58PCh. 21 - 22-71 Which amino acid side chain is most...Ch. 21 - 22-72 What does the reducing agent do in...Ch. 21 - 22-73 Silver nitrate is sometimes put into the...Ch. 21 - 22-74 Why do nurses and physicians use 70% alcohol...Ch. 21 - Prob. 63PCh. 21 - (Chemical Connections 21B ) AGE products become...Ch. 21 - Prob. 65PCh. 21 - Prob. 66PCh. 21 - Prob. 67PCh. 21 - Prob. 68PCh. 21 - Prob. 69PCh. 21 - 22-84 How many different dipeptides can be made...Ch. 21 - 22-85 Denaturation is usually associated with...Ch. 21 - Prob. 72PCh. 21 - Prob. 73PCh. 21 - Prob. 74PCh. 21 - 22-89 What kind of noncovalent interaction occurs...Ch. 21 - Prob. 76PCh. 21 - 22-91 Which amino acid does not rotate the plane...Ch. 21 - 22-92 Write the expected products of the acid...Ch. 21 - 22-93 What charges are on aspartic acid at pH 2.0?Ch. 21 - Prob. 80PCh. 21 - Prob. 81PCh. 21 - Prob. 82PCh. 21 - 22-97 Gelatin is derived from collagen by...Ch. 21 - Prob. 84PCh. 21 - Prob. 85PCh. 21 - Prob. 86PCh. 21 - 22-101 Using what you know about protein...Ch. 21 - 22-104 Why is collagen not a very good source of...Ch. 21 - Prob. 89P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
Most amino acids have isoelectric points between 5.0 and 6.0, but the isoelectric point of lysine is 9.7. Explain why lysine has such a high value for its isoelectric point.
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Using both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Pro
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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)
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22-71 Which amino acid side chain is most frequently involved in denaturation by reduction?
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Glutathione (G-SH), one of the most common tripeptides in animals, plants, and bacteria, is a scavenger of oxidizing agents. In reacting with oxidizing agents, glutathione is converted to G-S-S-G. (a) Name the amino acids in this tripeptide. (b) What is unusual about the peptide bond formed by the N-terminal amino acid? (c) Write a balanced half-reaction for the reaction of two molecules of glutathione to form a disulfide bond. Is glutathione a biological oxidizing agent or a biological reducing agent? (d) Write a balanced equation for reaction of glutathione with molecular oxygen, O2 to form G-S-S-G and H2O. Is molecular oxygen oxidized or reduced in this process?
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Draw Tryptophan in a peptide bond. Explain all of the bonds using valence bond theory (VBT). Next, explain where VBT fails and how molecular orbital theory is a better description of key regions of this amino acid and the peptide bonds it forms with other residues
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For lysine and arginine, the isoelectric point, pI, occurs at a pH where the net charge on the nitrogen-containing groups is +1 and balances the charge of -1 on the a-carboxyl group. Calculate pI for these amino acids.
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The pKa of the amino and carboxyl groups on alanine are 9.9 and 2.4, respectively. Under physiological conditions (pH 7.4), what percentage of alanine is ionized?
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The pKa for the side chain amino group in lysine is 10.4. If we were working at physiological pH 7.4, what would be the ratio of the protonated to unprotonated versions of lysine?
a.
1000:1
b.
3:1
c.
1:1000
d.
1:3
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Explain why the pI of lysine is the average of the pKa values of its two protonated amino groups.
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Consider a "tripeptide" with the following features (at pH = 10.8)
• The N-terminal amino acid is leucine
• The middle amino acid is aspartate
• The C-terminal amino acid is lysine
i. What is the 1-letter symbol for each of these amino acids
il. Calculate the net charge of the predominant ionic state of this tripeptide at
pH 10.8. Show work.
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Draw the peptide CHEMISTRY.
a. What is the full name and 3-letter abbreviation of this peptide?
b. Give the different forms (charges) of the peptide as it is titrated from pH 1.5 until pH 12.0.
c. What is the isoelectric point of the peptide?
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY