Given the oxygen dissociation curves, which of the following statements are correct?Which residue in HbA β do you think contributes the most to the increased interaction between HbA aand 2,3‑BPG? ### Oxygen Dissociation Curves**Graph Explanation:**The oxygen dissociation curves illustrate the relationship between oxygen partial pressure (\(pO_2\)) and the fractional saturation of oxygen (\(1/Y_{O2}\)). There are four curves representing different hemoglobin samples:- **HbA**: Normal adult hemoglobin- **HbF**: Fetal hemoglobin- **HbF + 2.5 mM BPG**: Fetal hemoglobin with 2.5 mM 2,3-BPG- **HbA + 2.5 mM BPG**: Normal adult hemoglobin with 2.5 mM 2,3-BPG- **HbA lysate****Key Observations:**- The curve for HbF is left-shifted compared to HbA, indicating higher oxygen affinity.- Addition of 2,3-BPG shifts both curves to the right, showing reduced affinity.**Questions:**- Evaluate the statements based on the dissociation curves: - Purified HbA has a higher oxygen affinity than purified HbF. - 2,3-BPG is an allosteric activator of HbA. - The allosteric effects of 2,3-BPG are homotropic. - 2,3-BPG only weakly interacts with HbF. - HbF loads oxygen at lower \(pO_2\) than does HbA in the presence of 2,3-BPG.### Sequence ComparisonThe researcher compares the sequences important for interaction with 2,3-BPG:- **HbA \(\beta\) Subunit Sequence (136-146)**: - GVNALAHKYH- **HbF \(\gamma\) Subunit Sequence (136-146)**: - AVASALSSRYH### Structure of 2,3-BPG- The molecular structure of 2,3-BPG is presented showing the phosphate groups, which play a key role in interacting with hemoglobin.### Discussion Question:- Which residue in HbA \(\beta\) do you think contributes the most to the increased interaction between HbA and 2,3-BPG?The set up is designed to encourage understanding of protein interactions, structural biology, and physiological implications of hemoglobin function. ### Hemoglobin and 2,3-BPG Interaction**Question:** Which residue in HbA β do you think contributes the most to the increased interaction between HbA and 2,3-BPG?**Options:** - Lys-144 - His-143 - Asn-139 - Ala-142 - Gly-136**Explanation:** This question is part of an educational module exploring the interaction between hemoglobin A (HbA) and 2,3-bisphosphoglycerate (2,3-BPG). Each option represents a distinct amino acid residue in the beta chain of hemoglobin. Understanding which residue contributes most to the interaction can provide insights into hemoglobin's oxygen-binding properties.

The binding of the oxygen molecule to a protein especially for transport or storage is known as…

HbF HbA + 2.5 mM BPG 1.0 Given the oxygen dissociation curves, which of the HbA, HbF + following statements are correct? 2.5 mM BPG 0.8 HbA lysate O Purified HbA has a higher oxygen affinity than purified HbF. 0.6 2,3-BPG is an allosteric activator of HbA. The allosteric effects of 2,3-BPG are homotropic. 0.4 2,3-BPG only weakly interacts with HbF. HbF loads oxygen at lower pO, than does HbA in the 0.2 presence of 2,3-BPG.

HbF HbA + 2.5 mM BPG 1.0 Given the oxygen dissociation curves, which of the HbA, HbF + following statements are correct? 2.5 mM BPG 0.8 HbA lysate O Purified HbA has a higher oxygen affinity than purified HbF. 0.6 2,3-BPG is an allosteric activator of HbA. The allosteric effects of 2,3-BPG are homotropic. 0.4 2,3-BPG only weakly interacts with HbF. HbF loads oxygen at lower pO, than does HbA in the 0.2 presence of 2,3-BPG.

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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