Answered: Will a mutation from Distal histidine…

Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?

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

See similar textbooks

Related questions

Q: In what general ways is balance of Ca21 achieved in the blood?

A: Calcium is of crucial importance in our body. It has several roles to play such as- Contraction…

Q: What determines the specificity of SH2 interactions with other molecules?

A: Introduction: to keep the macromolecule or polymers of biological molecules such as proteins intact,…

Q: From the figure of O2 binding to myoglobin and hemoglobin (ignore the line marked as T) as described…

A: The body receives nutrition, oxygen, and waste removal from the blood, which is a fluid that…

Q: The gamma and beta subunits that make up fetal and adult hemoglobin, respectively, differ in a…

A: BPG is 2,3-bisphosphoglycerate, which produced in the respiring tissue as a byproduct of glucose…

Q: Compared to maternal hemoglobin (HbA), fetal hemoglobin (HbF) has:

A: Fetal hemoglobin (HbF) is found in fetal red blood cells. The composition of fetal hemoglobin…

Q: What type of protein does FOG2 produce?

A: FOG 2 protein is coded by ZFPM 2. It is a family of transcription factors genes.

Q: Normal Hgb is referred to as HbA and contains 4 subunits, 2 α-globin chains and 2 β-globin chains,…

A: The protein structure has different levels:- Primary structure: refers to the normal amino acid…

Q: What are e-cigarettes? Why do you the CDC and other public health official’s are worried about kids…

A: Public Health refers to the health of the population as a whole. Organisations involved in…

Q: The cooperative binding behavior of hemoglobin for oxygen is best explained by...

A: Hemoglobin (Hb) is a protein molecule which is present in red blood cells and carries oxygen from…

Q: One of the treatments for sickle cell anemia is hydroxyurea, which is known to induce the expression…

A: The most important mutation is the third one where serine replaces histidine. Whereas histidine is…

Q: Compared to adult Hb (HbA), fetal Hb (HbF) has one less histidine in the central cavity where BPG…

A: Humans have both Hb A and Hb F hemoglobin which are present in adult and fetal life respectively.…

Q: Discuss that, what happens when Gαq proteins are stimulated?

A: We can say the proteins are the Ultimate player of gene expressions. Gɑq alpha proteins are…

Q: Hb Great Lakes 0.8 1. ;) The diagram on the right compares the O2 binding prop- erties or normal…

A: Hill plot for O2 binding to hemoglobin (Hb) has log(pO2) as X-axis and as Y-axis. We are given…

Q: Name four different proteins that facilitate the modification or folding of secretory proteins…

A: Several proteins facilitate the modification or folding of secretory proteins within the ER. These…

Q: Based on the UCP1 protein structure and the figure above, what are the likely chemical properties of…

A: UCP 1 protein: The UCP1 (uncoupling protein 1) protein is a mitochondrial protein found in brown…

Q: One of the molecules listed below is effective in reducing O2 affinity of human Hb in the absence of…

A: Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…

Q: Is there a better solution for treating hypercholesterolemia that statins

A: Hypercholesterolemia refers to the condition caused by the presence of high cholesterol in the body.…

Q: In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in…

A: Sickle cell disease is a blood condition that is most commonly found in the people of African…

Q: ckle cell anemia is a hereditary disease in which a faulty hemoglobin (Hb S) molecule is produced. A…

A: Hemoglobin is an iron-containing protein present in the red blood cells (RBCs). It transports oxygen…

Q: What's the role of VDAC1 mitochondrial protein in human diseases?

A: Mitochondrial proteins are proteins present within the mitochondria of cells, including within the…

Q: Certain individuals with mild forms ofβ-thalassemia produce, in addition to normal adulthemoglobin…

A: Haemoglobin lepore is defined as a small group consisting of structurally abnormal haemoglobins…

Q: Which factor determining the percent saturation of a binding site is the affinity of the binding…

A: Proteins are the polymers of amino acids. Proteins perform various functions in a cell. A protein is…

Q: Hemoglobin from different species can have different numbers of subunits. Let's consider three…

A: Hemoglobin (Hb) is the oxygen transport protein found in most vertebrates. Hb in nature exhibits…

Q: What will be the effect of the following changes to the protein structure of hemoglobin and its…

A: Hemoglobin is an oligomeric, allosteric, conjugated protein with four polypeptide chains. It…

Q: The following statements about the 'membrane attack complex' (MAC) is incorrect. Explain (i) The…

A: Introduction :- The membrane attack complex (MAC) or terminal complement complex (TCC) is a protein…

Q: Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and…

A: ANSWER;- It is given that the ka values of OBP and elephants Hb are the same at pH=7. Kd is the…

Q: Which of the following dephosphorylates PI 3,4,5-trisphosphate, thereby blocking the activation of…

A: The survival and growth is promoted by the PI3K-Akt signaling pathway. Protein Kinase B and…

Q: Atherosclerosis can obstruct or block flow in arteries, including those that provide oxygenated…

A: Artherosclerosis is a cardiovascular disorder caused due to build up of fat deposits in the walls of…

Q: The neighboring amino acid that TYR 368 interacts with is ILE 160. What are the properties of the…

A: Amino acids are natural mixes that contain amine and carboxyl functional groups, alongside a side…

Q: In a rare inherited disorder, called Wilson’s disease, excessive amounts of copper accumulate in…

A: It's an autosomal recessive disorder.

Q: Based on the following data, is the p50 higher or lower than normal in (a) hemoglobin Yakima and (b)…

A: P50 is defined as the oxygen tension at which haemoglobin is 50%saturated with oxygen .When…

Q: There was a study done (Isabel, et al.) on structural analysis of SARS-CoV-2 spike protein. The…

A: Hydrophobic groups are non-polar. These have a very low affinity with the polar groups. However,…

Q: A) 43 14 When Friend erythroleukemic cells are incubated with sodium butyrate, they differentiate…

A: Introduction : Histones are highly alkaline proteins. They are found in the nucleus of the…

Q: Briefly explain how heme regulates the expression of globin genes in cells that synthesize…

A: Hemoglobin synthesis are global production and heme synthesis. Globin chain production occurs in the…

Q: Amino acids at the interaction site ( F,I and L) and its G protein partner (P, L, Y) are very…

A: GPCRs are also known by the name of G Protein Coupled Receptors. These are integral membrane…

Q: How does the difference between the-chain and the -chain of hemoglobin explain the differences…

A: Hemoglobin is an oligomeric, allosteric, conjugated protein with four polypeptide chains joined by…

Q: 1. The shape of hemoglobin binding curves is: hyperbolic or sigmoidal 2. a) Based on the binding…

A: Note: As per the guidelines, i could solve only the first three subparts of the question. Please re…

Q: Fetal hemoglobin binds to BPG to a lesser extent than does HbA because His 143 in the BPG binding…

A: RBCs contain hemoglobin, the protein that transports oxygen from the lungs to our organs. The adult…

Question

Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1 Introduction

VIEW

Step 2 Answer and explanation

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Similar questions

What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.
What is the role of 2,3-BPG in O2 transfer from Maternal Hb to fetal Hb?
Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain astructural variant of hemoglobin, HbF, consisting of two α and two γ subunits (α2 γ2 ), whereas maternal erythrocytes contain HbA (α2β2).(a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain.(b) What is the physiological significance of the different O2 affinities?(c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2 -saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2 -saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of fetal and…
The haemoglobin proteins of RNA polymerase ii sub units RPB1-P24928 RPB2-P30876 RPB3-P19387 RPB4-015514 are they similar? Explain?
What are the properties provide that chaperone-mediated autophagy (CMA) is differentiated from other types of autophagy?
Can you check if A is correct and please help answer the following questions?
The ABO blood group antigens are the terminal sugars covalently linked to the end of the glycolipid in the red blood cellmembrane. The H antigen is the precursor of the A and Bantigens. Individuals with type A blood produce a gene thatcodes for an enzyme that adds N-acetylgalactosamine in ana(1,3) linkage to the Gal* residue in the H antigen. Type Bblood requires that an enzyme add a d-a galactose in an a(1,3) linkage to the Gal*. Draw the structures of the A andB antigens.
What is the effect of the altered amino acid sequence in Hb S that causes the cells to form sickle shapes?
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?
The mutation in hemoglobin at B82 Lys → Asp results in lowered O,-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site (see Figure 7.29; B82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, sug- gest a rationale for the observed reduction in Oz-binding affinity.
4)
Below is a list of hypothetical Hemoglobin variants. Circle the name of the variant that is most likely to show an increase in BPG binding. Does such a hypothetical variant cause an increase or decrease in hemoglobin's affinity for oxygen? A. Hb Miami: Leu is substituted with Pro in an alpha helix B. Hb California: Val is substituted with Lys at pH 7.0 C. Hb New york: Tyr is substituted with Met, which disrupts the hydrogen bonding at the a131 interface. D All of the above