Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Q23:
![**Transcription and Explanation for Educational Purposes**
**Title:** Molecular Interactions and Aggregation in Sickle-Cell Anemia
---
**Selection of Amino Acids for Pocket–Val 6 Interaction:**
Choose two amino acids that would be reasonable candidates for the pocket–Val 6 interaction.
- [ ] phenylalanine
- [ ] lysine
- [ ] glutamine
- [ ] glutamate
- [ ] leucine
**Explanation:** Selecting the correct amino acids is crucial for understanding protein interactions in sickle-cell disease. Focus on non-polar and hydrophobic properties that facilitate interactions with Valine 6.
---
**Understanding HbS Aggregation in Sickle-Cell Anemia:**
**Task:** Arrange the steps leading to hemoglobin S (HbS) aggregation in the correct order. Remember, deoxyhemoglobin (without oxygen) is in the T (tense) state, while oxyhemoglobin (with oxygen) is in the R (relaxed) state.
1. **R state Hb shifts to T state Hb.**
2. **[O₂] decreases due to vigorous exercise or high altitude.**
3. **Val interacts with the pocket of a β chain on another HbS.**
4. **Additional T state HbS interact with the growing aggregate to form an insoluble fiber.**
**Diagram Explanation:**
- **No aggregation:** Initially, the hemoglobin molecules do not aggregate, maintaining normal red blood cell shape.
- **Sickled red blood cell:** As hemoglobin aggregates due to the steps listed, red blood cells take on a sickled shape, characteristic of sickle-cell anemia.
**Answer Bank:**
- R state Hb shifts to T state Hb.
- Additional T state HbS interact with the growing aggregate to form an insoluble fiber.
- Val interacts with the pocket of a β chain on another HbS.
- [O₂] decreases due to vigorous exercise or high altitude.
**Note:** Understanding these molecular processes highlights the physiological changes in sickle-cell anemia, offering insights into therapeutic strategies.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa1e502f2-e187-4967-837b-da913ce1db1a%2Fdb3fcb7e-ddea-4e7c-9670-eed6346efc01%2Ftz25ew_processed.png&w=3840&q=75)
Transcribed Image Text:**Transcription and Explanation for Educational Purposes**
**Title:** Molecular Interactions and Aggregation in Sickle-Cell Anemia
---
**Selection of Amino Acids for Pocket–Val 6 Interaction:**
Choose two amino acids that would be reasonable candidates for the pocket–Val 6 interaction.
- [ ] phenylalanine
- [ ] lysine
- [ ] glutamine
- [ ] glutamate
- [ ] leucine
**Explanation:** Selecting the correct amino acids is crucial for understanding protein interactions in sickle-cell disease. Focus on non-polar and hydrophobic properties that facilitate interactions with Valine 6.
---
**Understanding HbS Aggregation in Sickle-Cell Anemia:**
**Task:** Arrange the steps leading to hemoglobin S (HbS) aggregation in the correct order. Remember, deoxyhemoglobin (without oxygen) is in the T (tense) state, while oxyhemoglobin (with oxygen) is in the R (relaxed) state.
1. **R state Hb shifts to T state Hb.**
2. **[O₂] decreases due to vigorous exercise or high altitude.**
3. **Val interacts with the pocket of a β chain on another HbS.**
4. **Additional T state HbS interact with the growing aggregate to form an insoluble fiber.**
**Diagram Explanation:**
- **No aggregation:** Initially, the hemoglobin molecules do not aggregate, maintaining normal red blood cell shape.
- **Sickled red blood cell:** As hemoglobin aggregates due to the steps listed, red blood cells take on a sickled shape, characteristic of sickle-cell anemia.
**Answer Bank:**
- R state Hb shifts to T state Hb.
- Additional T state HbS interact with the growing aggregate to form an insoluble fiber.
- Val interacts with the pocket of a β chain on another HbS.
- [O₂] decreases due to vigorous exercise or high altitude.
**Note:** Understanding these molecular processes highlights the physiological changes in sickle-cell anemia, offering insights into therapeutic strategies.
![The mutated form of hemoglobin (hemoglobin S, or HbS) in sickle-cell anemia results from the replacement of a glutamate residue by a valine residue at position 6 in the β chain of the protein. Normal hemoglobin is designated HbA.
Under conditions of low \([O_2]\), HbS aggregates and distorts the red blood cell into a sickle shape. See the image of eight aggregated HbS molecules. Sickled red blood cells are relatively inflexible and may clog capillary beds, causing pain and tissue damage. The sickled red blood cells also have a shorter life span, leading to anemia.
**Diagram Description:**
The image shows an aggregate of HbS molecules forming a distorted shape, indicating how HbS molecules clump together due to the valine-induced mutation.
**Question:**
Which amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6?
- [ ] arginine
- [ ] phenylalanine
- [ ] alanine
- [ ] lysine
- [ ] leucine
Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a β chain region located in the interior of the protein. In deoxyhemoglobin, however, this pocket is located on the surface of the protein. In deoxyhemoglobin S, Val 6 interacts with this surface pocket, leading to aggregation of HbS.
Choose two amino acids that would be reasonable candidates for the pocket–Val 6 interaction.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa1e502f2-e187-4967-837b-da913ce1db1a%2Fdb3fcb7e-ddea-4e7c-9670-eed6346efc01%2F2k5ys3_processed.png&w=3840&q=75)
Transcribed Image Text:The mutated form of hemoglobin (hemoglobin S, or HbS) in sickle-cell anemia results from the replacement of a glutamate residue by a valine residue at position 6 in the β chain of the protein. Normal hemoglobin is designated HbA.
Under conditions of low \([O_2]\), HbS aggregates and distorts the red blood cell into a sickle shape. See the image of eight aggregated HbS molecules. Sickled red blood cells are relatively inflexible and may clog capillary beds, causing pain and tissue damage. The sickled red blood cells also have a shorter life span, leading to anemia.
**Diagram Description:**
The image shows an aggregate of HbS molecules forming a distorted shape, indicating how HbS molecules clump together due to the valine-induced mutation.
**Question:**
Which amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6?
- [ ] arginine
- [ ] phenylalanine
- [ ] alanine
- [ ] lysine
- [ ] leucine
Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a β chain region located in the interior of the protein. In deoxyhemoglobin, however, this pocket is located on the surface of the protein. In deoxyhemoglobin S, Val 6 interacts with this surface pocket, leading to aggregation of HbS.
Choose two amino acids that would be reasonable candidates for the pocket–Val 6 interaction.
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