EP INTRO.TO GENERAL,ORGANIC...-OWL ACCE
12th Edition
ISBN: 9781337915984
Author: Bettelheim
Publisher: Cengage Learning
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Chapter 21, Problem 28P
Interpretation Introduction
Interpretation:
To find the number of ways the two amino acids, Serine and Glutamic acid can be linked to form a di-peptide.
Concept Introduction:
Amino acids link with each other by forming a peptide bond between them. The -NH2 group of one amino acids react with the -COOH group of the other amino acid to form a −CONH (peptide) bond.
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EP INTRO.TO GENERAL,ORGANIC...-OWL ACCE
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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- 22-62 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_forward22-53 Do iron and zinc ions play role in protein structure? If so, what is the role for either or both?arrow_forward22-49 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_forward
- For the tripeptide SerArgIle which amino acid residues a. are hydrophilic b. are hydrophobic c. possess polar neutral R groups d. participate in two amide linkagesarrow_forwardWhat functional groups are found in all amino acids? How many different amino acids are found in naturally occurring proteins?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_forward
- Which of the following are true concerning the chemical bond that forms between the carboxyl (RCOOH) group of one amino acid and the amino (RCNH2) group of another? a.The bond is called a peptide bond. b.It is formed by inserting a water molecule between them. c.It is formed by a dehydration reaction. d.A polypeptide has more of these bonds than a protein.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_forward21-101 Glycerophospholipids tend to have both a positive charge and a negative charge in their hydrophilic portions. Does this fact help or hinder lipid packing in membranes? Explain.arrow_forward
- For the tripeptide AlaValGly which amino acid residues, if any, a. are hydrophilic b. are hydrophobic c. possess nonpolar R groups d. participate in two amide linkagesarrow_forwardUsing 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_forwardWhich of the following describes the primary structure of proteins? a. The collective shape assumed by all of the chains in a protein containing multiple chains. b. The folding of an individual protein molecule. c. The regular repeated shape of the protein molecules backbone. d. The sequence of amino acids bonded together by peptide bonds.arrow_forward
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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