CHEMISTRY (LOOSELEAF) >CUSTOM<
13th Edition
ISBN: 9781264348992
Author: Chang
Publisher: MCGRAW-HILL HIGHER EDUCATION
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Chapter 25, Problem 25.17QP
Interpretation Introduction
Interpretation:
The phenomenon of cooperativity exhibited by the hemoglobin molecule in binding of oxygen has to be explained.
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1. What are the solubility characteristics
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Why is there a thermodynamic push toward enzyme-substrate complex formation when a nonpolar substrate binds to the nonpolar active site of an enzyme?
Oxygen is transported around the body by the globular protein hemoglobin which contains
four Fe2* ions. Hemoglobin is “oxygenated" when coordinated to dissolved oxygen in the
blood. This can be simplistically represented by the following equation (where Hb represents
one hemoglobin molecule):
н (ад) + 402 (д) + нь(02)4 (аq) (1)
Hemoglobin also readily binds with carbon monoxide (CO). Indeed, hemoglobin has a much
higher affinity to CO than O2 resulting in significantly stronger hemoglobin binding to CO than
to O2. This is a problem because hemoglobin molecules which are coordinated to carbon
monoxide are unable to transport oxygen around the body as needed. No more than 2.5% of
your body's hemoglobin can be bound to CO before health effects become noticeable. The
consequence is that even very low partial pressures of CO in the air have physiological
implications for humans.
нь (ад) + 4Cо (д) + нь(со)4 (аq)
(2)
Compare and evaluate the relative magnitudes of the equilibrium constant for…
Chapter 25 Solutions
CHEMISTRY (LOOSELEAF) >CUSTOM<
Ch. 25 - Prob. 25.1QPCh. 25 - Prob. 25.2QPCh. 25 - Prob. 25.3QPCh. 25 - Prob. 25.4QPCh. 25 - Prob. 25.5QPCh. 25 - Prob. 25.6QPCh. 25 - Prob. 25.7QPCh. 25 - Prob. 25.8QPCh. 25 - Prob. 25.9QPCh. 25 - Prob. 25.10QP
Ch. 25 - Prob. 25.11QPCh. 25 - Prob. 25.12QPCh. 25 - Prob. 25.13QPCh. 25 - Prob. 25.14QPCh. 25 - Prob. 25.15QPCh. 25 - Prob. 25.16QPCh. 25 - Prob. 25.17QPCh. 25 - Prob. 25.18QPCh. 25 - Prob. 25.19QPCh. 25 - Prob. 25.20QPCh. 25 - Prob. 25.21QPCh. 25 - Prob. 25.22QPCh. 25 - Prob. 25.23QPCh. 25 - Prob. 25.24QPCh. 25 - Prob. 25.25QPCh. 25 - Prob. 25.26QPCh. 25 - Discuss the importance of hydrogen bonding in...Ch. 25 - Proteins vary widely in structure, whereas nucleic...Ch. 25 - Prob. 25.29QPCh. 25 - Prob. 25.30QPCh. 25 - Prob. 25.31QPCh. 25 - Prob. 25.32QPCh. 25 - Prob. 25.33QPCh. 25 - Prob. 25.34QPCh. 25 - Prob. 25.35QPCh. 25 - Chemical analysis shows that hemoglobin contains...Ch. 25 - Prob. 25.37QPCh. 25 - What kind of intermolecular forces are responsible...Ch. 25 - Draw structures of the nucleotides containing the...Ch. 25 - Prob. 25.40QPCh. 25 - Prob. 25.41QPCh. 25 - Prob. 25.42QPCh. 25 - Prob. 25.43QPCh. 25 - Prob. 25.44QPCh. 25 - When deoxyhemoglobin crystals are exposed to...Ch. 25 - Prob. 25.46QPCh. 25 - Prob. 25.47QPCh. 25 - Prob. 25.48QPCh. 25 - Prob. 25.49QPCh. 25 - Prob. 25.50QPCh. 25 - Prob. 25.51QPCh. 25 - Assume the energy of hydrogen bonds per base pair...Ch. 25 - Prob. 25.53QP
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- 22-65 (a) What is the difference in the quaternary structure between fetal hemoglobin and adult hemoglobin? (b) Which can carry more oxygen? (c) What would the oxygen saturation curve of fetal hemoglobin look like compared to that of myoglobin and regular adult hemoglobin?arrow_forwardThe process by which an enzyme acts on the substrate can be described by the: a. lock-and-key model. b. enzyme-and-substrate model. c. enzyme folding model. d. catalytic model.arrow_forwardDescribe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.arrow_forward
- Would alpha-D-glucopyranose and alpha-D-fructopyranose be equally likely to be the substrate for a given enzyme? Refer to both shape and noncovalent interactions in your answer. Make one generalization about protein-carbohydrate interactionsarrow_forwardThe mutated form of hemoglobin (hemoglobin S, or HbS) in sickle-cell anemia results from the replacement of a glutamate residue by a valine residue at position 6 in the ß chain of the protein. Normal hemoglobin is designated HbA. Under conditions of low [O₂], HbS aggregates and distorts the red blood cell into a sickle shape. See image of eight aggregated HbS molecules. Sickled red blood cells are relatively inflexible and may clog capillary beds, causing pain and tissue damage. The sickled red blood cells also have a shorter life span, leading to anemia. Which amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6? arginine phenylalanine Aggregate of HbS molecules lysine leucine alanine Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a B chain ranion located in the interior of the neotain In daaxshamaalahin homauar thic nookat is laastad on the curfona of tha 0arrow_forwardTwo-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intracellular abundance. Describe a quantitative approach to determine the number of molecules of an enzyme per cell.arrow_forward
- Plot the enzyme activity (absorbance) versus pH. From this curve, what is the optimal pH? Explain why enzyme activities depend on the pH. Similarly plot the enzyme activity versus temperature. Report the optimal temperature. Discuss why do you choose this optimal temperature and pH.arrow_forwardWhich statement does NOT apply to the lock-and-key theory? O explains the functioning of enzymes explains the need for a specific three dimensional structure found in proteins explains the reason why a particular enzyme is involved with one substrate explains why a substrate-enzyme complex is so difficult to separatearrow_forwardWhat is an antioxidant enzyme? Why is catalase considered to be an antioxidant enzyme?arrow_forward
- nineyarrow_forwardDifferentiate and explain the chemical basis of the Kjeldahl, Lowry and Bradford techniques that can be used to quantitate proteins in quality control and research.arrow_forwardComplete the sentence to make it true. The single most important contribution to the stability of a water soluble globular protein's conformation appears to be the sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein. entropy increase from the decrease in the number of ordered water molecules forming a solvent shell around the unfolded protein. sum of free energies of formation of many weak interactions between a protein's polar amino acids and surrounding water. maximum enthalpy increase from ionic interactions between the ionized amino acids in a protein. stabilizing effect of hydrogen bonding in a protein between the carbonyl group of one peptide bond and the amino group of anotherarrow_forward
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