a.What is the difference between the 5th and 6 coordination sites in the heme group?

Q: Starting from the O2 binding equilibrium of human hemoglobin written below, derive the Hb + nO2 2…

A: Hemoglobin is an oligomeric conjugated protein with four peptide chains joined by a non-covalent…

Q: What is the function of hemoglobin subunit beta?

A: Hemoglobin chain is composed of four heme groups that forms a tetrahedral structure. It is a pigment…

Q: Which of the following statements is false concerning the structure of hemoglobin?

A:

Q: how many moles of oxygen could be transported by the hemoglobin complex formed from 8 mg of dietary…

A: Hemoglobin (Hb) is the protein molecule, which consists of the complex which exhibits the Fe…

Q: Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and…

A: Hemoglobin is the most important iron-containing component found in the RBC or in blood. They are…

Q: What is the biological advantage to the sigmoidal binding curve of hemoglobin for oxygen? A. It…

A: The binding of oxygen to the haemoglobin increases with increase in oxygen partial pressure, Maximum…

Q: A. Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF?…

A: Hemoglobin: It is the respiratory pigment present in the red blood cells and gives the red color to…

Q: Describe the structure of a hemoglobin molecule. Explain where O2 and CO2 are carried on a…

A: Hemoglobin is an oxygen-transport metalloprotein that consists of iron. In blood, it carries oxygen…

Q: Explain how the oxygen dissociation curve is related to the properties and function of hemoglobin

A: Introduction: Hemoglobin is a globular protein with four polypeptide chains bonded together. It has…

Q: Diagram the methemoglobin reductase pathway and explain its importance in maintaining functional…

A: Red blood cells contain hemoglobin that carries oxygen from the lungs to the body's tissues and…

Q: Which of the following statements about the Istate of hemoglobin is FALSE? a. iron ion is pulled to…

A: Hemoglobin is the protein of RBCs that bind oxygen and is a globular protein having quaternary…

Q: . When all the BPG is carefully removed from samples of HbA and HbF, the measured O2-saturation…

A: BPG is a bisphospho glyceric acid present in RBC. It has different affinities for oxygenated…

Q: Considering the quantity of hemoglobin in an erythrocyte and the oxygen-binding properties of…

A: Blood is a body fluid in other animals and humans. It supplies necessary substances to the cells,…

Q: 3. Explain the Right shift and Left shift as seen in the Hemoglobin-oxygen dissociation curve with…

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

Q: The hemoglobin of a human fetus differs from adult hemoglobin. Compare the dissociation curves of…

A: hemoglobin is the protein which helps in transport of oxygen in bloodstream .

Q: Define how carbaminohemoglobin (HbCO2) is formed ?

A: Haemoglobin (Hb) is a quaternary protein found in the red blood cells (RBCs) that carries oxygen and…

Q: Why people with PK deficiency may tolerate a lower hemoglobin level than people with other types of…

A: Pyruvate kinase deficiency (PKD) is the most prevalent congenital glycolysis enzymatic abnormality…

Q: A) describe in molecular detail how protonation of the histidine side-chain results in hemoglobin's…

A: Hemoglobin is the primary protein responsible for the transport of oxygen from lungs to different…

Q: Which of the following is true about the T (tense)  -->R (relaxed) transition of hemoglobin? A. The…

A: Hemoglobin is described as a very important protein that is present in our RBCs. They have the role…

Q: Explain the advantages and disadvantages of a respiratory pigment with relatively low O2 affinity in…

A: Respiratory pigments are carriers of oxygen in the body of the organism. In humans and most mammals,…

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: Suggest a way in which the difference between the functions of hemoglobin and myoglobin is reflected…

A: Hemoglobin, in the red blood cells, carries oxygen throughout the body. Myoglobin is an iron and…

Q: What is the allosteric effect on O2 binding to the second subunit of hemoglobin after the first…

A: Haemoglobin can bind hydrogen ion, oxygen molecule and carbon dioxide to itself. All these bindings…

Q: What is the critical amino acid difference between the beta-chain and the gamma-chain of hemoglobin?…

A: Haemoglobin A is the adult haemoglobin tetramer composed of 2 alpha and 2 beta chains whereas fetal…

Q: Describe the effect of 2,3- bisphosphoglycerate on the binding of oxygen by hemoglobin.

A: Hemoglobin is a heterotetrameric protein. It carries iron at its core. it is responsible for the…

Q: After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the…

A: Air enters the lungs through the oral cavity or nasal passage, which join together in the pharynx.…

Q: How does the nature try to prevent a contact between carbon monoxide and hemoglobin? On the other…

A: Oxygen is required for the generation of ATPs in all the metabolically active cells of the body and…

Q: The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2)…

A: The activity of molecule 2,3 phosphoglycerate (BPG) is important to obtain stabilized structure of…

Q: a) draw the scheme of ETC and describe the structure of its components; b) explain how the…

A: Answer of A ): diagram above  The electron transport chain is a series of 4 protein complexes that…

Q: One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin…

A: BPG is 2,3 -biphosphoglycerate binds to the hemoglobin.

Q: O, saturation curve is shown below for hemoglobin at various pHs. Detail this Bohr effect from the…

A: Hemoglobin is an allosteric protein. It facilitates the transport of oxygen and carbon dioxide in…

Q: What would happen in terms of pH, T to R state stability, and oxygen-carrying capacity if…

A: Whenever hemoglobin binds to oxygen there is conformational change occurs called the oxygenated…

Q: Determine which statements apply to hemoglobin, myoglobin, or neither (you can write in the…

A: Haemoglobin is the molecule which is present in the blood and carries oxygen to the tissues and…

Q: Oxygen has an allosteric interaction with hemoglobin. What are the results of this interaction as…

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

Q: Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and…

A: Hemoglobin is the protein present in red blood cells to carry oxygen throughout our body and carbon…

Q: Briefly explain why fetal Hb has a higher affinity for O2 when compared to the adult Hb

A: The haemoglobin pigment, which is found in red blood cells and gives blood its red colour, is known…

Q: Why chemical change occurs in the primary structure of the globin portionof the hemoglobin molecule…

A: Globin is a protein component of hemoglobin (part of red blood cell which carries oxygen to…

Q: A. Circle the distal Histidine residue. B. What is the function of the distal Histidine residue? C.…

A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…

Q: Which of the following statements about the Istate of hemoglobin is FALSE? O a, iron ion is pulled…

A: Hemoglobin binds and transports oxygen from the lungs to the body tissues. It is found in red blood…

Q: You are studying with a friend who is describing the Bohr effect. She tells you that in the lungs,…

A: In 1904, a Danish physiologist named Christian Bohr proposed a theory known as  Bohr effect. He…

Q: In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin…

A: Oxygen binds to hemoglobin in reversible manner, specific changes in the surrounding environment…

Q: Compare the three spectra. What can you observe when the starting hemoglobin is diluted? Does the…

A: Given : Absorbance 1<Absorbance 2<Absorbance 3

Q: Below is a list of hypothetical Hemoglobin variants. Circle the name of the variant that is most…

A: Hemoglobin exists in the T and R state during the absence and presence of oxygen respectively. In…

Q: People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major…

A: Hemoglobin is the iron-containing pigment in the red blood cells which helps the blood to carry or…

Q: Describe the effect of 2, 3-bisphosphoglycerate on the binding of oxygen by hemoglobin.

A: 2, 3-Bisphosphoglycerate (2,3-BPG) is most abundant organic phosphate in the red blood cell.…

Q: Increasing concentrations of either 2,3-bisphosphoglycerate (BPG) or protons (H +) cause a…

A: Need to find whether increasing concentration of BPG Cause a rightward or leftward shift of oxygen…

Hematology

Hematology is the branch of biology. Hematology is the medical field that deals with the treatment of blood disorders and cancers, such as hemophilia, leukemia, lymphoma, and sickle-cell anemia. Hematologists and hematopathologists are medical professionals who specialize in illnesses of the blood and its components.