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OWLv2 for Bettelheim/Brown/Campbell/Farrell/Torres' Introduction to General, Organic and Biochemistry, 11th Edition, [Instant Access], 1 term (6 months)
11th Edition
ISBN: 9781305106734
Author: Frederick A. Bettelheim; William H. Brown; Mary K. Campbell; Shawn O. Farrell; Omar Torres
Publisher: Cengage Learning US
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Textbook Question
Chapter 22, Problem 22.43P
22-43 (a) Draw the structural formula of the tripeptide Met—Ser—Cys.
(b) Draw the different ionic structures of this tripeptide at pH 2.0, 7.0, and 10.0.
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Chapter 22 Solutions
OWLv2 for Bettelheim/Brown/Campbell/Farrell/Torres' Introduction to General, Organic and Biochemistry, 11th Edition, [Instant Access], 1 term (6 months)
Ch. 22.4 - Problem 22-1 Show how to form the dipeptide...Ch. 22.10 - Problem 22-2 What is the oxidation number (the...Ch. 22.10 - Prob. 22.3PCh. 22.11 - Prob. 22.4PCh. 22 - 22-5 What are the functions of (a) ovalbumin and...Ch. 22 - 22-6 The members of which class of proteins are...Ch. 22 - 22-7 What is the function of an immunoglobulin?Ch. 22 - Prob. 22.8PCh. 22 - 22-9 What is the difference in structure between...Ch. 22 - 22-10 Classify the following amino acids as...
Ch. 22 - 22-11 Which amino acid has the highest percentage...Ch. 22 - Prob. 22.12PCh. 22 - Prob. 22.13PCh. 22 - Prob. 22.14PCh. 22 - Prob. 22.15PCh. 22 - 22-16 Which amino acids in Table 22-1 have more...Ch. 22 - 22-17 What are the similarities and differences in...Ch. 22 - 22-18 Draw the structures of L- and D-valine.Ch. 22 - Prob. 22.19PCh. 22 - 22-20 Show how alanine, in solution at its...Ch. 22 - 22-21 Explain why an amino acid cannot exist in an...Ch. 22 - 22-22 Draw the structure of valine at pH 1 and at...Ch. 22 - Prob. 22.23PCh. 22 - 22-24 Draw the most predominant form of histidine...Ch. 22 - 22-25 Draw the most predominant form of lysine at...Ch. 22 - Prob. 22.26PCh. 22 - 22-27 Show by chemical equations how alanine and...Ch. 22 - 22-28 A tetrapeptide is abbreviated as DPKH. Which...Ch. 22 - 22-29 Draw the structure of a tripeptide made of...Ch. 22 - 22-30 (a) Use the three-letter abbreviations to...Ch. 22 - 22-31 A polypeptide chain is made of alternating...Ch. 22 - Prob. 22.32PCh. 22 - 22-33 Which of the three functional groups on...Ch. 22 - Prob. 22.34PCh. 22 - 22-35 Why is histidine considered a basic amino...Ch. 22 - Prob. 22.36PCh. 22 - Prob. 22.37PCh. 22 - 22-38 Why does proline not absorb light at 280 nm?Ch. 22 - Prob. 22.39PCh. 22 - Prob. 22.40PCh. 22 - Prob. 22.41PCh. 22 - 22-42 (a) How many atoms of the peptide bond lie...Ch. 22 - 22-43 (a) Draw the structural formula of the...Ch. 22 - 22-44 How can a protein act as a buffer?Ch. 22 - 22-45 Proteins are least soluble at their...Ch. 22 - 22-46 How many different tripeptides can be made...Ch. 22 - 22-47 How many different tetrapeptides can be made...Ch. 22 - 22-48 How many amino acid residues in the A chain...Ch. 22 - 22-49 Based on your knowledge of the chemical...Ch. 22 - 22-50 Is a random coil a (a) primary, (b)...Ch. 22 - 22-51 Decide whether the following structures that...Ch. 22 - Prob. 22.52PCh. 22 - 22-53 Do iron and zinc ions play role in protein...Ch. 22 - Prob. 22.54PCh. 22 - 22-55 Consider the coordination compound Fe(CO)5...Ch. 22 - Prob. 22.56PCh. 22 - 22-57 Consider the coordination compound...Ch. 22 - Prob. 22.58PCh. 22 - 22-59 What is the effect of salt bridges on the...Ch. 22 - Prob. 22.60PCh. 22 - 22-61 Polyglutamic acid (a polypeptide chain made...Ch. 22 - 22-62 Distinguish between intermolecular and...Ch. 22 - 22-63 Identify the primary, secondary, and...Ch. 22 - 22-64 If both cysteine residues on the B chain of...Ch. 22 - 22-65 (a) What is the difference in the quaternary...Ch. 22 - Prob. 22.66PCh. 22 - Prob. 22.67PCh. 22 - Prob. 22.68PCh. 22 - Prob. 22.69PCh. 22 - Prob. 22.70PCh. 22 - 22-71 Which amino acid side chain is most...Ch. 22 - 22-72 What does the reducing agent do in...Ch. 22 - 22-73 Silver nitrate is sometimes put into the...Ch. 22 - 22-74 Why do nurses and physicians use 70% alcohol...Ch. 22 - 22-75 (Chemical Connections 22A) Why must some...Ch. 22 - Prob. 22.76PCh. 22 - Prob. 22.77PCh. 22 - Prob. 22.78PCh. 22 - Prob. 22.79PCh. 22 - Prob. 22.80PCh. 22 - Prob. 22.81PCh. 22 - 22-82 (Chemical Connections 22H) How does the...Ch. 22 - Prob. 22.83PCh. 22 - 22-84 How many different dipeptides can be made...Ch. 22 - 22-85 Denaturation is usually associated with...Ch. 22 - Prob. 22.86PCh. 22 - Prob. 22.87PCh. 22 - Prob. 22.88PCh. 22 - 22-89 What kind of noncovalent interaction occurs...Ch. 22 - Prob. 22.90PCh. 22 - 22-91 Which amino acid does not rotate the plane...Ch. 22 - 22-92 Write the expected products of the acid...Ch. 22 - 22-93 What charges are on aspartic acid at pH 2.0?Ch. 22 - Prob. 22.94PCh. 22 - Prob. 22.95PCh. 22 - Prob. 22.96PCh. 22 - 22-97 Gelatin is derived from collagen by...Ch. 22 - Prob. 22.98PCh. 22 - Prob. 22.99PCh. 22 - Prob. 22.100PCh. 22 - 22-101 Using what you know about protein...Ch. 22 - Prob. 22.102PCh. 22 - Prob. 22.103PCh. 22 - 22-104 Why is collagen not a very good source of...Ch. 22 - Prob. 22.105P
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- Using the single letter abbreviations A, V, and L, as given in Table 22-1, list the tripeptides formed if alanine, valine, and leucine are all mixed together and peptide bonds are allowed to form in all possible combinations.arrow_forward22-84 How many different dipeptides can be made (a) using only alanine, tryptophan, glutamic acid, and arginine and (b) using all 20 amino acids?arrow_forward22-62 Distinguish between intermolecular and intramolecular hydrogen bonding between backbone groups. Where in protein structures do you find one, and where do you find the other?arrow_forward
- 22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a substitution for leucine in the primary structure of a protein that would probably not change the character of the protein very much.arrow_forward21-90 To what extent do lipids and carbohydrates play structural roles in living organisms? Do these roles differ in plants and in animals?arrow_forward22-53 Do iron and zinc ions play role in protein structure? If so, what is the role for either or both?arrow_forward
- 22-46 How many different tripeptides can be made (a) using one, two, or three residues each of leucine, threonine, and valine and (b) using all 20 amino acids?arrow_forward22-85 Denaturation is usually associated with transitions from helical structures to random coils. If an imaginary process were to transform the keratin in your hair from an (-helix to a (-pleated sheet structure, would you call the process denaturation? Explain.arrow_forward22-47 How many different tetrapeptides can be made (a) if the peptides contain the residues of asparagine, proline, serine, and metbionine and (b) if all 20 amino acids can be used?arrow_forward
- 22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forward22-20 Show how alanine, in solution at its isoelectric point, acts as a buffer (write equations to show why the pH does not change much if we add an acid or a base).arrow_forward21-3 Proteins, nucleic acids, and carbohydrates are grouped by common structural features found within their group. What is the basis for grouping substances as lipids?arrow_forward
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