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
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 22, Problem 22.95P
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.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Chapter 22 Solutions
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
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- 22-53 Do iron and zinc ions play role in protein structure? If so, what is the role for either or both?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_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
- 22-45 Proteins are least soluble at their isoelectric points. What would happen to a protein precipitated at its isoelectric point if a few drops of dilute HCl were added?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_forward22-101 Using what you know about protein denaturation, what is one reason you must maintain a body temperature in a strict range?arrow_forward
- 22-104 Why is collagen not a very good source of dietary 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_forward22-44 How can a protein act as a buffer?arrow_forward
- Quaternary protein structure is more easily disrupted than tertiary protein structure. Explain why this is so.arrow_forward22-50 Is a random coil a (a) primary, (b) secondary, (c) tertiary or (d) quaternary structure? Explain.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
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning
Chemistry: An Atoms First ApproachChemistryISBN:9781305079243Author:Steven S. Zumdahl, Susan A. ZumdahlPublisher:Cengage Learning
ChemistryChemistryISBN:9781305957404Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCostePublisher:Cengage Learning
Chemistry: Matter and ChangeChemistryISBN:9780078746376Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl WistromPublisher:Glencoe/McGraw-Hill School Pub Co
World of ChemistryChemistryISBN:9780618562763Author:Steven S. ZumdahlPublisher:Houghton Mifflin College Div
Introduction to General, Organic and Biochemistry
Chemistry
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Cengage Learning
Chemistry: An Atoms First Approach
Chemistry
ISBN:9781305079243
Author:Steven S. Zumdahl, Susan A. Zumdahl
Publisher:Cengage Learning
Chemistry
Chemistry
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Cengage Learning
Chemistry: Matter and Change
Chemistry
ISBN:9780078746376
Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl Wistrom
Publisher:Glencoe/McGraw-Hill School Pub Co
World of Chemistry
Chemistry
ISBN:9780618562763
Author:Steven S. Zumdahl
Publisher:Houghton Mifflin College Div
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY