Concept explainers
(a)
Interpretation:
The function or biological activity of insulin in the body should be determined.
Concept Introduction:
The primary structure of protein is the sequence of amino acids. The a-helix and β-sheet structure are the secondary structures. Similarly tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds etc. which get altered after heating or in the presence of certain chemicals. Hence these structures get changed during denaturation of protein.
(b)
Interpretation:
The function or biological activity of myoglobin in the body should be determined.
Concept Introduction:
The primary structure of protein is the sequence of amino acids. The a-helix and β-sheet structure are the secondary structures. Similarly tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds etc. which get altered after heating or in the presence of certain chemicals. Hence these structures get changed during denaturation of protein.
(c)
Interpretation:
The function or biological activity of a-keratin in the body should be determined.
Concept Introduction:
The primary structure of protein is the sequence of amino acids. The a-helix and β-sheet structure are the secondary structures. Similarly tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds etc. which get altered after heating or in the presence of certain chemicals. Hence these structures get changed during denaturation of protein.
(d)
Interpretation:
The function or biological activity of chymotrypsin in the body should be determined.
Concept Introduction:
The primary structure of protein is the sequence of amino acids. The a-helix and β-sheet structure are the secondary structures. Similarly tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds etc. which get altered after heating or in the presence of certain chemicals. Hence these structures get changed during denaturation of protein.
(e)
Interpretation:
The function or biological activity of oxytocin in the body should be determined.
Concept Introduction:
The primary structure of protein is the sequence of amino acids. The a-helix and β-sheet structure are the secondary structures. Similarly tertiary and quaternary structures also have certain weak intermolecular forces. These structures have different intermolecular forces between peptide chains like hydrogen bonds, S-S bonds etc. which get altered after heating or in the presence of certain chemicals. Hence these structures get changed during denaturation of protein.
Want to see the full answer?
Check out a sample textbook solutionChapter 21 Solutions
General, Organic, & Biological Chemistry
- 22-53 Do iron and zinc ions play role in protein structure? If so, what is the role for either or both?arrow_forwardWhat special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?arrow_forward22-48 How many amino acid residues in the A chain of insulin are the same in insulin from humans, cattle (bovine), hogs, and sheep?arrow_forward
- Which is NOT a characteristic of proteins? a. They contain genetic information. b. They can act as hormones. c. They can catalyze chemical reactions. d. They act in cell membrane trafficking.arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forward22-91 Which amino acid does not rotate the plane of polarized light?arrow_forward
- Consider the tripeptide leucylvalyltryptophan. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has a basic side chain?arrow_forwardGive one example of a conjugated protein that contains the following prosthetic group: a.iron b.lipid c.phosphate group d.carbohydrate e.hemearrow_forward21-3 Proteins, nucleic acids, and carbohydrates are grouped by common structural features found within their group. What is the basis for grouping substances as lipids?arrow_forward
- Describe the process by which blood immunoglobulins help protect the body from invading bacteria and viruses.arrow_forward21-85 Which of the following statements is (are) consistent with what is known about membranes? (a) A membrane consists of a layer of proteins sandwiched between two layers of lipids. (b) The compositions of the inner and outer lipid layers are the same in any individual membrane. (c) Membranes contain glycolipids and glycoproteins. (d) Lipid bilayers are an important component of membranes. (e) Covalent bonding takes place between lipids and proteins in most membranes.arrow_forwardConsider the tripeptide tyrosylleucylisoleucine. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has an acidic side chain?arrow_forward
- Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage LearningIntroduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage LearningGeneral, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
- Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,Chemistry: Matter and ChangeChemistryISBN:9780078746376Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl WistromPublisher:Glencoe/McGraw-Hill School Pub CoWorld of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage Learning