**Title: Understanding Sickle Cell Disease and Hemoglobin Structure**Figure 9 illustrates changes to the beta-globin subunit of hemoglobin in sickle cell disease and the functional consequence for red blood cells. This image has been modified in accordance with a Creative Commons License.**Image Explanation:**The image demonstrates two scenarios:- **Normal Hemoglobin:** - Partial Amino Acid Sequence for Beta Globin: Pro-Glu-Glu - Hemoglobin Molecule: Represented by a cluster of circular shapes. - Red Blood Cell: A standard round shape.- **Sickle Cell Disease:** - Partial Amino Acid Sequence for Beta Globin: Pro-Val-Glu - Hemoglobin Molecule: A similar cluster to the normal but depicts a variation. - Red Blood Cell: A crescent or sickle shape.**Educational Activity:**1. **Video Engagement:** - Watch a video on sickle cell anemia and then answer the questions provided.2. **Discussion Questions:** - **3. Molecular Cause of Sickle Cell Disease:** - A valine is substituted for a glutamate in hemoglobin, initiating sickle cell disease. - Consider which levels of protein structure are altered. - Analyze specific interactions changing in protein shape. - **4. Functional Implications in Red Blood Cells:** - Normal cells travel efficiently through blood vessels, whereas sickle-shaped cells get stuck, causing anemia. - Discuss the relationship between amino acid sequence, protein shape, and function in an organism.**Activity Table:**The table below summarizes the findings related to protein structure through the activity:| Protein Structure Level | Types of Bonds Generated to Reinforce that Level | Groups of Amino Acids Contributing to the Bonds | Key Terms/Ideas Defining that Level ||-------------------------|--------------------------------------------------|-------------------------------------------------|------------------------------------|| | | | || | | | || | | | || | | | |Complete the table as you engage with the educational content, providing detailed insights into protein structure levels and their importance. **Quaternary Structure**One final level of structure exists for some, but not all, proteins. This is called **quaternary structure**. Proteins that have quaternary structure are formed from two or more polypeptides that assemble into one active structure. The different polypeptides in a protein with quaternary structure are often called **subunits**. These subunits may be identical or different. One example of a protein with quaternary structure is hemoglobin, the protein that transports oxygen in our blood. The structure of hemoglobin is shown in Figure 8.**Figure 8**. Quaternary structure of hemoglobin with labeled subunits. Note: each subunit contains one non-protein heme group complexed to an oxidized iron atom (Fe2+). These “prosthetic groups” are required for carrying oxygen in the blood. Modified from this link under Creative Commons license.**Answer the below questions on quaternary structure in your own document.**1. Based on your interpretation of Figure 9, how many subunits does hemoglobin contain? Are they all the same or different?2. Which types of interactions do you think stabilize the quaternary structure of proteins that have this level of structure? (Hint: this is not any different from the interactions you identified in tertiary structure, except for the fact that multiple polypeptides are involved).

Protein structure has many levels such as primary, secondary, tertiary and quaternary. Hemoglobin is…

Red Blood Cell: Figure 9. Changes to the beta-globin subunit of hemoglobin in sickle cell disease and the functional consequence for red blood cells. Image modified from here in accordance with Creative Commons License. Watch this video about sickle cell anemia, then answer the questions below. 3. Figure 9 illustrates the molecular cause of the most common version of sickle cell disease. A valine is substituted for a glutamate in hemoglobin in sickle cell disease. Which levels of protein structure are altered, and specifically, which types of interaction are likely to be changed in determining the shape of the protein? Explain your answer. 4. Normal red blood cells can easily travel through blood vessels, whereas sickle- shaped red blood cells get stuck. This is the basis of sickle cell anemia. What does this tell you about the relationship between the sequence of amino acids, the shape of the protein and its function in a cell/organism? mmarize what you found for each level

Red Blood Cell: Figure 9. Changes to the beta-globin subunit of hemoglobin in sickle cell disease and the functional consequence for red blood cells. Image modified from here in accordance with Creative Commons License. Watch this video about sickle cell anemia, then answer the questions below. 3. Figure 9 illustrates the molecular cause of the most common version of sickle cell disease. A valine is substituted for a glutamate in hemoglobin in sickle cell disease. Which levels of protein structure are altered, and specifically, which types of interaction are likely to be changed in determining the shape of the protein? Explain your answer. 4. Normal red blood cells can easily travel through blood vessels, whereas sickle- shaped red blood cells get stuck. This is the basis of sickle cell anemia. What does this tell you about the relationship between the sequence of amino acids, the shape of the protein and its function in a cell/organism? mmarize what you found for each level

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 19QP: Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the...

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Similar questions

Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.
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