Introduction to General, Organic and Biochemistry
11th Edition
ISBN: 9781285869759
Author: Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher: Cengage Learning
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Chapter 22, Problem 22.99P
Interpretation Introduction
Interpretation:
The reason behind the fact that amino acids such as histidine, aspartic acid, and serine found more often near the reaction catalysis site than amino acids such as leucine and valine is to be stated.
Concept Introduction:
The amino acids are the functional unit of proteins. The different amino acids combine to form a wide range of proteins. Protein is required to maintain various activities and
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Introduction to General, Organic and Biochemistry
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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- 22-61 Polyglutamic acid (a polypeptide chain made only of glutamic acid residues) has an a-helix conformation below pH 6.0 and a random-coil conformation above pH 6.0. What is the reason for this conformational change?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_forward22-31 A polypeptide chain is made of alternating valine and phenylalanine. Which part of the polypeptide is polar (hydrophilic)?arrow_forward
- 22-47 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_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_forward22-46 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_forward
- 22-89 What kind of noncovalent interaction occurs between the following amino acids? (a) Valine and isoleucine (b) Glutamic acid and lysine (c) Tyrosine and threonine (d) Alanine and alaninearrow_forward22-97 Gelatin is derived from collagen by denaturation. Is a gelatin dessert likely to be a good source of dietary protein?arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forward
- 22-9 What is the difference in structure between tyrosine and phenylalanine?arrow_forward22-50 Is a random coil a (a) primary, (b) secondary, (c) tertiary or (d) quaternary structure? Explain.arrow_forward22-92 Write the expected products of the acid hydrolysis of the following tetrapeptide:arrow_forward
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