A) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of thehistidine side chain.b) what is the pKa of the histidine side-chain ionizable group expected to have?|

Introduction: Hemoglobin is the major protein responsible for transporting oxygen from the lungs to…

Answered: A) llustrate in molecular detail how…

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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Titration of alanine by a strong base, for example NaOH, reveals two pk's. Which is the titration reaction occurring at pK1 (pK1 = %3D 2.34)? O-NH2 + COH →-NH + H2O O-COOH + OH →-CO + H20 -COOH + -NH2 → -COO" + -NH2+ -CoO +-NH2* → -COOH +-NH2 O -NH3* + OH →-NH2 + H2O
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How does the difference between the-chain and the -chain of hemoglobin explain the differences inoxygen binding between Hb A and Hb F?
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The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2) facilitating the reversible release of oxygen. Approximate relationships between BFG concentrations in red blood cells and Pos in hemoglobin are in the table.a) Draw the reaction schemeb) Write the forces that condition the union between hemoglobin and BFG
1. Researchers isolated a monomeric protein from platelets that has 2 binding sites (A and B) for ADP; Site A's Ka is 157 μM, and Site B's Kd is 2.2 μM. 1.1. A) Which binding site has higher affinity for ADP? B) Briefly justify your answer. C) For this higher affinity site, calculate the standard free energy change for ADP binding. Show your work. 1.2. What concentration of ADP is required to get site A filled in 20% of the proteins? 1.3. Based on this information, sketch a graph of the fraction of site B filled as a function of [ADP].
Please fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to the
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
( please give answer in simple language and draw diagram where necessary) do 1st question
What qualitative effect would you expect each of the following to have on the Ps0 of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chains

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A) llustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?