Chemistry Answer the following questions about hemoglobin. The number of high affinity binding sites in the R form of hemoglobin is The number of low affinity binding sites in the R form of hemoglobin is -- The number of 02 molecules that need to bind to convert hemoglobin from the T to R form is The number of high affinity binding sites in the T form of hemoglobin is __- The number of low affinity binding sites in the T form of hemoglobin is

Chemistry Answer the following questions about hemoglobin. The number of high affinity binding sites in the R form of hemoglobin is The number of low affinity binding sites in the R form of hemoglobin is -- The number of 02 molecules that need to bind to convert hemoglobin from the T to R form is The number of high affinity binding sites in the T form of hemoglobin is __- The number of low affinity binding sites in the T form of hemoglobin is

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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A person was found to have very low levels of functional beta globin mRNA and therefore very low levels of the beta globin protein. What problems would this cause for assembling functional haemoglobin molecules?
How does hemoglobin bind O2 cooperatively? A. The binding of one molecule of O2 to one subunit of hemoglobin enhances the assembly of other subunits to form a complete hemoglobin protein. B. The binding of one molecule of O2 to one hemoglobin protein enhances the binding of a molecule of O2 to a different hemoglobin protein. C. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of the same subunit for more molecules of O2. D. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of other subunits for O2.
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).
Fill in the blank: Hemoglobin S moves more slowly toward the positive electrode than hemoglobin A on an electrophoresis gel at pH 9.2, because hemoglobin S has ____ __________ negative charges than hemoglobin A.
Sketch out the binding site of Hemoglobin with oxygen bound . ( You can abstract the Heme ring out i.e. not draw each chemical bond). Please label both imported HIS residues.
Your friend's genetic test revealed that they have a rare mutation - they lack the glycotransferase responsible for adding the terminal fucose molecule to the oligosaccharide on the surface of red blood cells. What is the consequence for a blood transfusion - which blood groups can they receive donations from, if any? Why? Although they lack the terminal fucose normally found on the surface of red blood cells, can you make any predictions as to wheter they also have or lack the Galactose or GalNAc found on A or B blood types? Your friend suggested a simpler way to test for this type of mutation. They have suggested taking a Fucosidase (a type of glycosidase) and mutating it so that the active site was no longer functional - they claim this would endow the protein with the properties of a lectin. Does their claim make any sense?
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)
Which of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.
The classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109erythrocytes will form a monolayer of area 0.89 m2when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2in area. Show that these data can be accounted for only if the erythrocyte membrane is a bilayer.
The amino acid in Hemoglobin that is most found to be most sensitive to pH changes, and hence affects Oxygen binding process around pH 7 is Valine Tyrosine Histidine Aspartic Acid
The classic demonstration that cell plasma membranes are composed ofbilayers depends on the following kinds of data:• The membrane lipids from 4.74 x 109 erythrocytes will form a monolayerof area 0.89 m2 when spread on a water surface.• The surface of one erythrocyte is approximately 100 μm2 in area.Show that these data can be accounted for only if the erythrocyte membraneis a bilayer.
Use the image below to answer this question and the three questions that follow: a) what is the correct description of the hemoglobin for Paul? b) Where is the + pole of the electrophoresis for the gel shown in the previous question? c) Refer to gel illustration above. Which of the following statements provides the best explanation for the difference in mobility of HbA and HbS? 1) HbA is larger in size than HbS 2) HbA is smaller in size than HbS 3) HbA has less negative charge than HbS under electrophoretic conditions used 4) HbA is smaller and more negatively charged under the electrophoretic conditions used 5) HbA is larger and has a less negative charge under the electrophoretic conditions used, whereas HbS is smaller and has a more negative charge