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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Chapter 21, Problem 81P
Interpretation Introduction
Interpretation:
The effects of disulphide bond formation on the structure of proteins should be explained.
Concept Introduction:
Amino acids being dipolar molecules are present as zwitterions in water. In the aqueous solution, they show both positive and negative charges. Positive charge will be acquired by -NH2 group being basic in nature and negative charge is acquired by -COOH group being acidic in nature. If both acidic and basic groups are ionized, zwitterion is formed. The pH at this stage is known as isoelectric point.
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✓ edict the products of this organic reaction:
----
။
A
CH3–C−NH–CH2–C−CH3 + KOH
?
Specifically, in the drawing area below draw the condensed structure of the product, or products, of this reaction. If there's more
than one product, draw them in any arrangement you like, so long as they aren't touching.
If there aren't any products because this reaction won't happen, check the No reaction box under the drawing area.
Explanation
Check
Click anywhere to draw the first
atom of your structure.
C
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Predict the product of this organic reaction:
A
HO-C-CH3 + CH3NH2
P+ H2O
Specifically, in the drawing area below draw the condensed structure of P.
If there is no reasonable possibility for P, check the No answer box under the drawing area.
Explanation
Check
Click anywhere to draw the first
atom of your structure.
m
H
1) OsO4, pyridine
2) Na2SO3 or
NaHSO3 in H₂O
2 products
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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