Concept explainers
(a)
Interpretation:
The graph of the given data to form an oxygen-binding curve is to be plotted. The oxygen partial pressure at which the given hemoglobin is half-saturated is to be stated. Whether oxygen binding seems to be cooperative or not on the basis of the curve is to be stated.
Concept introduction:
Proteins are the
Answer to Problem 16P
The plot of the given data to form an oxygen-binding curve is shown below.
The oxygen partial pressure at which the given hemoglobin is half-saturated is
Explanation of Solution
On the basis of the given data for oxygen-binding for lamprey hemoglobin, the graph of fractional saturation versus partial pressure of oxygen is plotted as follows:
At the oxygen partial pressure,
Thus, this plot between partial pressure of oxygen
(b)
Interpretation:
A hill plot by using the given data is to be stated. Whether the hill plot shows any evidence for cooperativity or not is to be stated. The information about the hill coefficient is to be explained.
Concept introduction:
Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well.
The hill equation indicates the two close equations which show the binding of a ligand with the macromolecule.
Answer to Problem 16P
A hill plot by using the given data is shown as,
This plot show little bit cooperativity in the center of the curve and its hill coefficient is
Explanation of Solution
The equation that is used to show the hill equation is given as,
Here,
The values of
Similarly, for
The value of
Similarly, for
With the help of the given data for oxygen-binding for lamprey hemoglobin, the plot between
The value of slope
The hill coefficient for the graph is
(c)
Interpretation:
A model that is used to explain the observed cooperativity in oxygen binding by lamprey hemoglobin is to be stated.
Concept introduction:
Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well.
Answer to Problem 16P
A model that is used to explain the observed cooperativity in oxygen binding by lamprey hemoglobin suggests that binding of oxygen with any monomer is easier as compared to binding of first oxygen with deoxygenated dimer.
Explanation of Solution
It is given that lamprey hemoglobin produces oligomers in the deoxygenated state. These oligomers were primarily dimmers in the deoxygenated state. These dimers are having low affinity for oxygen as compared to monomers. The cooperativity in oxygen binding is shown only if the dissociation of dimmers into two monomers occurs after the binding of first oxygen atom with a dimer. In this model, the binding of oxygen with every monomer is very easy as compared to the binding between first oxygen and the deoxy dimer.
Want to see more full solutions like this?
Chapter 7 Solutions
SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
- Biochemistry Question Please help. Thank you What is the function of glutamate dehydrogenase?arrow_forwardBiochemistry Question Please help. Thank you How and why does a high protein diet affect the enzymes of the urea cycle?arrow_forwardBiochemistry What is the importance of the glucose-alanine cycle?arrow_forward
- Biochemistry Assuming 2.5 molecules of ATP per oxidation of NADH/(H+) and 1.5molecules of ATP per oxidation of FADH2, how many ATP are produced per molecule of pyruvate? Please help. Thank youarrow_forward1. How would you explain the term ‘good food’? 2. How would you define Nutrition? 3. Nutrients are generally categorised into two forms. Discuss.arrow_forwardBiochemistry Question. Please help solve. Thank you! Based upon knowledge of oxidation of bioorganic compounds and howmuch energy is released during their oxidation, rank the following, from most to least, with respect to how much energy would be produced from each during their oxidation. Explain your placement for each one.arrow_forward
- Biochemistry Question.For the metabolism of amino acids what is the first step for theirbreakdown? Why is it necessary for this breakdown product to be transported to the liver? For the catabolism of the carbon backbone of these amino acids, there are 7 entry points into the “standard” metabolic pathways. List these 7 entry points and which amino acids are metabolized to these entry points. Please help. Thank you!arrow_forwardBiochemistry Question. Please help. Thank you. You are studying pyruvate utilization in mammals for ATP production under aerobic conditions and have synthesized pyruvate with Carbon #1 labelled with radioactive C14. After only one complete cycle of the TCA cycle, which of the TCA cycle intermediates would be labeled with C14? Explain your answer. Interestingly, you find C14 being excreted in the urine. How does it get there?arrow_forwardBiochemistry question. Please help with. Thanks in advance For each of the enzymes listed below, explain what the enzyme does including function, names (or structures) of the substrate and products and the pathway(s) (if applicable) it is/are found in. (a) ATP synthetase (b) succinate dehydrogenase (c) isocitrate lyase (d) acetyl CoA carboxylase (e) isocitrate dehydrogenase (f) malate dehydrogenasearrow_forward
- Draw and name each alcohol and classify it as primary, secondary, or tertiary. Explain your answer thoroughly.arrow_forwardDraw the product of each reaction. If there are multiple products, draw only the major product. Explain your answer thoroughly.arrow_forwardIdentify the type of bond in the following disaccharides. Number your carbons to show work. Explain your answer thoroughly. Draw the number of carbons also.arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON