Instructor Manual for Anatomy & Physiology 1st Edition Elizabeth Co Complete Chapter 1 - 28

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Instructor Manual for Anatomy & Physiology 1st Edition Elizabeth Co Complete Chapter 1 - 28

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2026/2027

Institution Anatomy And Physilogy

Course Anatomy and physilogy

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Solutions Manual and Answer Guide for Anatomy and Physiology 1st Edition Elizabeth Co Apply to Pathophysiology Questions, Section 3.5d: Sickle Cell Anemia: 1. d. Both B and C Bloom’s level: Understand Rationale: Proteins fold into unique three-dimensional shapes, which determine the functions of the proteins. Many physiological changes, such as pH and temperature, unfold or denature proteins and therefore prevent them from functioning. Ligand binding can induce shape changes in proteins; some ligands activate protein function, while others inhibit them from functioning. Protein shape has a profound effect on the functioning of proteins. The amino acid sequence represents the primary structure of proteins, but the three-dimensional shape (tertiary structure) determines the actual shape of the protein and, therefore, its function. 2. c. The proteins would be drawn together and tend to clump. Bloom’s level: Analyze Rationale: The mutated proteins would be drawn together and tend to clump. In nature, polar molecules are attracted to other polar molecules, while nonpolar molecules cluster with other nonpolar molecules. When glutamic acid is replaced by valine in the mutated hemoglobin molecules in people with sickle cell anemia, the valine molecules are attracted to other valine molecules in nearby hemoglobin molecules, causing them to clump together. The mutated proteins have a different orientation in red blood cells; therefore, they change the shape of the cells from round to crescentshaped. 3. d. All of the above could be plausible. Bloom’s level: Apply Rationale: All of the above are possible. A misfolded (denatured) protein may not be able to bind to its ligand because its binding site is no longer exposed or has been repositioned to the interior of the protein. In some cases, the shape change may increase the affinity of the protein for its ligand. Learning Check Questions, Section 3.5d: 1. a. Amino group b. Carboxyl group c. Central carbon atom Bloom’s level: Remember Rationale: A carboxyl group and amino group are bound to a central carbon atom to form an amino acid. 2. a. Amino acid peptide protein

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