EP INTRO.TO GENERAL,ORGANIC...-OWL ACCE
EP INTRO.TO GENERAL,ORGANIC...-OWL ACCE
12th Edition
ISBN: 9781337915984
Author: Bettelheim
Publisher: Cengage Learning
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Chapter 21, Problem 1P

22-5 What are the functions of (a) ovalbumin and (b) myosin?

Expert Solution
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Interpretation Introduction

(a)

Interpretation:

The functions of ovalbumin should be explained.

Concept Introduction:

An organic compound derived from two amino acids is known as dipeptide. The amino acids can be same or different. There are different ways by which amino acids can join to form a protein. The order of amino acid decides the type of protein. The bond between two amino acids to form a dipeptide is a peptide bond.

Answer to Problem 1P

Ovalbumin is known to be a storage protein.

Explanation of Solution

Ovalbumin is found in egg white, it makes 55% of the total protein. Its function is not known but it is assumed to be a storage protein.

Expert Solution
Check Mark
Interpretation Introduction

(b)

Interpretation:

The functions of myosin should be explained.

Concept Introduction:

An organic compound derived from two amino acids is known as dipeptide. The amino acids can be same or different. There are different ways by which amino acids can join to form a protein. The order of amino acid decides the type of protein. The bond between two amino acids to form a dipeptide is a peptide bond.

Answer to Problem 1P

Myosin plays an important role in the contraction of muscles and processes involved in movement of one substance to other in eukaryotes.

Explanation of Solution

Myosin is ATP- dependent and plays an important role in the contraction of muscle and mobile processes in the cells of eukaryotes.

They are restricted to muscle cells but important for binding of actin, hydrolysis of ATP and force transduction.

There are myosin isoforms present in all the eukaryotic cells and they have specialized functions depending on the type of muscles they are present in.

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Chapter 21 Solutions

EP INTRO.TO GENERAL,ORGANIC...-OWL ACCE

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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