2. (a)The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo-globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group ofthe BPG molecule confer strong, negative electrostatic character to the molecule.B₁-subunit1.2.3.5.6.B₁(b)Mutant HemoglobinHb RaleighHb HelsinkiThe mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or inthe vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for bindingBPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for HbRaleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substitutedby Ala.Hb RahereHb Rancho MirageHb Little RockB₂Hb OhioMutationVal (31)AlaLys(382) MetLys(382)) ThrHis(143)AspHis(3143)Glna-NHẠAla(142)AspHis 2His 143BPGHis 143Lys 82His 2Rank the affinity of the mutant hemoglobins for binding BPG.a-NH,*B2-subunitExplanation of effect of mutation on BPGbinding

To comprehend the BPG binding site within hemoglobin, it's important to note that it resides within…

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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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Antithrombin III forms an irreversible complex with thrombin but not with prothrombin. What is the most likely reason for this difference in reactivity?
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
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)
Give detailed Solution with explanation (no need Handwritten
5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION
HbA1c is a glycated hemoglobin in which a glucose molecule is covalently bound to the N-terminal valine of a hemoglobin subunit. True False
CO2 Iragment (interinediary) to slaction transport chain CH Pyruvate -Krebs/citric acid cycle COA COO CH C - S CH2 HO C CO" CH2 Acetyi CoA CH COO CH2 HS-COA H0-CH NADH HC CH2 NAD+ Oxaloacetate Citrate HO-CH Isocitrate NAD+ Malate NADH CO H20- CH a-Ketoglutarate CH2 HC NAD+ Fumarate NADH CH2 COO O2 FADH FAD Suceinyl CoA Succinate COO GTP GDP CO" 1. CH: PO. CH2 CH2 CH2 GTP 1. S COA GDP COO ADP ATP iii. An acyl-group transfer can be seen twice in the cycle. The first time when -SCOA group on acetyl- COA is replaced with OH from water (which then is
In one type of hemoglobin variant, lysine EF6 is replaced by an aspartic acid residue. What would be the effects of this mutation on the affinity of the hemoglobin for 2,3 BPG and oxygen? The affinity for 2,3-BPG would increase, and for oxygen would decrease. The affinity for 2,3-BPG would decrease, and for oxygen would decrease. The affinities for 2,3-BPG and for oxygen would be unaffected. The affinity for 2,3-BPG would increase, and for oxygen would increase. The affinity for 2,3-BPG would decrease, and for oxygen would increase.
You have discovered a new hemoglobin variant you are calling Hb-21. You have noticed the following from your studies of Hb-21: - The binding constant of Hb-21 is the same at pH 7.1 and 7.4.- The binding constant curves generated by Hb-21 and O2 are sigmoidal.- The Hill coefficient for Hb-21 is 3.-The binding constant for Hb-21 with O2 in the presence of 5mM 2,3-bisphosphglycerate is about 6-times lower instead of the 8-times lower that is observed under these conditions for the wild type enzyme. Use this information to answer questions: Based on this information which of these features of hemoglobin would you conclude are altered in Hb-21 as compared to the wild type hemoglobin? ____ the cooperativity.____ the amount of T versus R state in the tissues. ____ the Bohr effect. What is the major issue for an individual with the Hb-21 variant? Explain exactly what aspect of hemoglobin’s function is altered.
Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?
Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2

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