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The following sequence alignment shows the point mutation that exists in hemoglobin for some cases of sickle cell (HbS) compared to wild type adult hemoglobin (HbA) VLSPADK (HBA) VLSPAVK (HbS) Based solely on the peptide fragment shown, answer the following questions: What is the charge range for the HbA peptide shown above? **Hint, what is convention for how charge ranges are written?? At physiological pH, what is the charge of the HbS peptide? →>> What is the impact of this point mutation? Choose the letter for the answer choice that best applies. a. Allows for hydrophobic contacts in HbS that lead to higher order structures beyond the a2ß2 heterotetramer b. Allows for ionic interactions in HbS that aids in interactions with solvent c. Destabilizes the ionic interactions of the dimer-dimer interface and prevents the T- to R- state transition d. Prevents the coordination of Fe²+ at the protoporphyrin ring

The following sequence alignment shows the point mutation that exists in hemoglobin for some cases of sickle cell (HbS) compared to wild type adult hemoglobin (HbA) VLSPADK (HBA) VLSPAVK (HbS) Based solely on the peptide fragment shown, answer the following questions: What is the charge range for the HbA peptide shown above? **Hint, what is convention for how charge ranges are written?? At physiological pH, what is the charge of the HbS peptide? →>> What is the impact of this point mutation? Choose the letter for the answer choice that best applies. a. Allows for hydrophobic contacts in HbS that lead to higher order structures beyond the a2ß2 heterotetramer b. Allows for ionic interactions in HbS that aids in interactions with solvent c. Destabilizes the ionic interactions of the dimer-dimer interface and prevents the T- to R- state transition d. Prevents the coordination of Fe²+ at the protoporphyrin ring

Human Anatomy & Physiology (11th Edition)
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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The following sequence alignment shows the point mutation that exists in hemoglobin for some cases of sickle cell (HbS) compared to wild type adult hemoglobin (HbA) VLSPADK (HBA) VLSPAVK (HbS) Based solely on the peptide fragment shown, answer the following questions: What is the charge range for the HbA peptide shown above? **Hint, what is convention for how charge ranges are written?? At physiological pH, what is the charge of the HbS peptide? →>>> What is the impact of this point mutation? Choose the letter for the answer choice that best applies. a. Allows for hydrophobic contacts in HbS that lead to higher order structures beyond the a2ß2 heterotetramer b. Allows for ionic interactions in HbS that aids in interactions with solvent c. Destabilizes the ionic interactions of the dimer-dimer interface and prevents the T- to R- state transition d. Prevents the coordination of Fe²+ at the protoporphyrin ring
Transcribed Image Text:The following sequence alignment shows the point mutation that exists in hemoglobin for some cases of sickle cell (HbS) compared to wild type adult hemoglobin (HbA) VLSPADK (HBA) VLSPAVK (HbS) Based solely on the peptide fragment shown, answer the following questions: What is the charge range for the HbA peptide shown above? **Hint, what is convention for how charge ranges are written?? At physiological pH, what is the charge of the HbS peptide? →>>> What is the impact of this point mutation? Choose the letter for the answer choice that best applies. a. Allows for hydrophobic contacts in HbS that lead to higher order structures beyond the a2ß2 heterotetramer b. Allows for ionic interactions in HbS that aids in interactions with solvent c. Destabilizes the ionic interactions of the dimer-dimer interface and prevents the T- to R- state transition d. Prevents the coordination of Fe²+ at the protoporphyrin ring
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