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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.
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Chapter 21 Solutions
EBK GENERAL, ORGANIC, & BIOLOGICAL CHEM
- 22-48 How many amino acid residues in the A chain of insulin are the same in insulin from humans, cattle (bovine), hogs, and sheep?arrow_forwardWhich 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_forward
- 22-91 Which amino acid does not rotate the plane of polarized light?arrow_forwardConsider 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_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,World of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage LearningChemistry: Principles and PracticeChemistryISBN:9780534420123Author:Daniel L. Reger, Scott R. Goode, David W. Ball, Edward MercerPublisher:Cengage Learning
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