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Questions and Answers
Which transition metal binds well to O2 but would generate free radicals if free in solution?
Which transition metal binds well to O2 but would generate free radicals if free in solution?
- Magnesium (Mg)
- Iron (Fe+) (correct)
- Zinc (Zn)
- Copper (Cu)
What evolutionary solution is mentioned for capturing the oxygen molecule safely?
What evolutionary solution is mentioned for capturing the oxygen molecule safely?
- Directly binding oxygen with protein side chains
- Binding oxygen with heme that is protein bound (correct)
- Using free Fe2+ ions
- Utilizing organometallic compounds like Fe3+
Which type of structure is myoglobin?
Which type of structure is myoglobin?
- Lipid structure
- Nucleic acid structure
- Carbohydrate structure
- Protein structure (correct)
What is the role of the 'proximal' His in myoglobin structure?
What is the role of the 'proximal' His in myoglobin structure?
Why does CO bind better to free heme than O2?
Why does CO bind better to free heme than O2?
What factor contributes to CO binding about 200x less effectively than O2 in the middle of the protein?
What factor contributes to CO binding about 200x less effectively than O2 in the middle of the protein?
How does protein structure affect ligand binding?
How does protein structure affect ligand binding?
What is one reason why lowering the affinity (P50) of myoglobin to oxygen would not help in delivering oxygen to tissues?
What is one reason why lowering the affinity (P50) of myoglobin to oxygen would not help in delivering oxygen to tissues?
What is the consequence of the formation of a carbamate in hemoglobin?
What is the consequence of the formation of a carbamate in hemoglobin?
What distinguishes hemoglobin from myoglobin in terms of oxygen binding?
What distinguishes hemoglobin from myoglobin in terms of oxygen binding?
Which factor leads to the release of oxygen in the tissues?
Which factor leads to the release of oxygen in the tissues?
What is required for positive cooperativity in hemoglobin's affinity for oxygen?
What is required for positive cooperativity in hemoglobin's affinity for oxygen?
What role does H+ play in oxygen transport by hemoglobin?
What role does H+ play in oxygen transport by hemoglobin?
What does a sigmoidal binding curve indicate in terms of ligand cooperativity?
What does a sigmoidal binding curve indicate in terms of ligand cooperativity?
What is the quantitative description of cooperativity represented by in a Hill plot?
What is the quantitative description of cooperativity represented by in a Hill plot?
How does a drop in pH affect hemoglobin's affinity for oxygen?
How does a drop in pH affect hemoglobin's affinity for oxygen?
What contributes to the efficiency of oxygen transport in the body?
What contributes to the efficiency of oxygen transport in the body?
What percentage of carbon dioxide is exported in the form of a carbamate on the amino terminal residues of hemoglobin subunits?
What percentage of carbon dioxide is exported in the form of a carbamate on the amino terminal residues of hemoglobin subunits?
What does a small equilibrium dissociation constant (Kd) indicate?
What does a small equilibrium dissociation constant (Kd) indicate?
Which of the following is NOT a component of a heme group?
Which of the following is NOT a component of a heme group?
What characterizes the specificity of proteins in binding to ligands?
What characterizes the specificity of proteins in binding to ligands?
Which type of proteins undergo conformational changes upon ligand binding, allowing for tighter binding?
Which type of proteins undergo conformational changes upon ligand binding, allowing for tighter binding?
How is the equilibrium composition characterized in terms of the equilibrium constant Ka?
How is the equilibrium composition characterized in terms of the equilibrium constant Ka?
What does the heme-bound FE cation represent in myoglobin?
What does the heme-bound FE cation represent in myoglobin?
What triggers the conformational change from the T to R state in hemoglobin?
What triggers the conformational change from the T to R state in hemoglobin?
Which state of hemoglobin has a higher affinity for oxygen?
Which state of hemoglobin has a higher affinity for oxygen?
What does the binding of O2 cause in the hemoglobin subunits?
What does the binding of O2 cause in the hemoglobin subunits?
Who determined the structures of hemoglobin in the presence and absence of Oxygen?
Who determined the structures of hemoglobin in the presence and absence of Oxygen?
What is hypothesized to cause the significant conformational change in hemoglobin upon Oxygen binding?
What is hypothesized to cause the significant conformational change in hemoglobin upon Oxygen binding?
What does the binding of O2 in the hemoglobin subunit's pocket trigger?
What does the binding of O2 in the hemoglobin subunit's pocket trigger?
What does Linus Pauling discover that helps lower the standard state free energy change of a reaction?
What does Linus Pauling discover that helps lower the standard state free energy change of a reaction?
In enzymatic catalysis, what is the role of the catalytic triad in chymotrypsin?
In enzymatic catalysis, what is the role of the catalytic triad in chymotrypsin?
What is the function of the acyl-enzyme intermediate in enzymatic reactions?
What is the function of the acyl-enzyme intermediate in enzymatic reactions?
How does the catalytic triad in chymotrypsin contribute to the catalytic mechanism of the enzyme?
How does the catalytic triad in chymotrypsin contribute to the catalytic mechanism of the enzyme?
Which of the following is a key feature of peptide bond formation catalyzed by enzymes like chymotrypsin?
Which of the following is a key feature of peptide bond formation catalyzed by enzymes like chymotrypsin?
What is the primary function of water activation in enzymatic reactions like those catalyzed by chymotrypsin?
What is the primary function of water activation in enzymatic reactions like those catalyzed by chymotrypsin?
What is the role of Asp-102 in the catalytic triad of chymotrypsin?
What is the role of Asp-102 in the catalytic triad of chymotrypsin?
What does Ser-195 do in the catalytic triad of chymotrypsin?
What does Ser-195 do in the catalytic triad of chymotrypsin?
Why does His-57 interact with Serine in chymotrypsin catalysis?
Why does His-57 interact with Serine in chymotrypsin catalysis?
In chymotrypsin catalysis, what is the function of the catalytic triad in breaking peptide bonds?
In chymotrypsin catalysis, what is the function of the catalytic triad in breaking peptide bonds?
Which statement accurately describes the oxyanion hole in chymotrypsin?
Which statement accurately describes the oxyanion hole in chymotrypsin?
What is the main function of the acyl-enzyme intermediate in chymotrypsin catalysis?
What is the main function of the acyl-enzyme intermediate in chymotrypsin catalysis?
What is the primary function of a Lewis base?
What is the primary function of a Lewis base?
In acid-base catalysis, what role does water typically play?
In acid-base catalysis, what role does water typically play?
Why might general acid-base catalysis be preferred over specific acid-base catalysis?
Why might general acid-base catalysis be preferred over specific acid-base catalysis?
Which amino acid side chain is not usually ionizable and involved in general acid-base catalysis?
Which amino acid side chain is not usually ionizable and involved in general acid-base catalysis?
What is the main requirement for general acid-base catalysis when proton transfer from water is slow?
What is the main requirement for general acid-base catalysis when proton transfer from water is slow?
What is the role of histidine in the catalytic triad of chymotrypsin?
What is the role of histidine in the catalytic triad of chymotrypsin?
In enzyme catalysis, what is the purpose of the amino acid group in general acid-base catalysis?
In enzyme catalysis, what is the purpose of the amino acid group in general acid-base catalysis?
What is the function of the aspartate residue in chymotrypsin's active site?
What is the function of the aspartate residue in chymotrypsin's active site?
What occurs during the burst phase in chymotrypsin catalysis?
What occurs during the burst phase in chymotrypsin catalysis?
What is the purpose of water activation in chymotrypsin catalysis?
What is the purpose of water activation in chymotrypsin catalysis?
Which residue in chymotrypsin is responsible for stabilizing the transition state during catalysis?
Which residue in chymotrypsin is responsible for stabilizing the transition state during catalysis?
What effect does His have on water molecules during chymotrypsin catalysis?
What effect does His have on water molecules during chymotrypsin catalysis?
How do general acids and bases help increase the rate of a reaction in enzyme catalysis?
How do general acids and bases help increase the rate of a reaction in enzyme catalysis?
What is one role of covalent catalysis in enzyme catalysis?
What is one role of covalent catalysis in enzyme catalysis?
What amino acids can act as nucleophiles involved in covalent catalysis?
What amino acids can act as nucleophiles involved in covalent catalysis?
In chymotrypsin, what accelerates peptide bond hydrolysis?
In chymotrypsin, what accelerates peptide bond hydrolysis?
What is the role of the catalytic triad in chymotrypsin for peptide bond hydrolysis?
What is the role of the catalytic triad in chymotrypsin for peptide bond hydrolysis?
How does acyl-enzyme intermediate formation contribute to enzyme catalysis?
How does acyl-enzyme intermediate formation contribute to enzyme catalysis?
What does the turnover number, kcat, represent?
What does the turnover number, kcat, represent?
What is the approximate measure of substrate's affinity for enzyme known as?
What is the approximate measure of substrate's affinity for enzyme known as?
Why is Km often compared to Kd?
Why is Km often compared to Kd?
Which enzyme has a turnover number of approximately 40 million per second?
Which enzyme has a turnover number of approximately 40 million per second?
What is the significance of a lower Km value in enzyme kinetics?
What is the significance of a lower Km value in enzyme kinetics?
In enzyme kinetics, what does Kcat measure?
In enzyme kinetics, what does Kcat measure?
Which assumption underlies the comparison between Km and Kd?
Which assumption underlies the comparison between Km and Kd?
What does Km represent in terms of substrate concentration and enzymatic reaction?
What does Km represent in terms of substrate concentration and enzymatic reaction?
What are the factors that can affect the rate of an enzymatic reaction?
What are the factors that can affect the rate of an enzymatic reaction?
What is the primary purpose of studying enzyme kinetics?
What is the primary purpose of studying enzyme kinetics?
In enzyme assay example with Alcohol Dehydrogenase (ADH), why is NADH production monitored at 340 nm?
In enzyme assay example with Alcohol Dehydrogenase (ADH), why is NADH production monitored at 340 nm?
What does the process of making mutations in enzymes aim to determine?
What does the process of making mutations in enzymes aim to determine?
How are kinetic parameters determined in enzyme kinetics studies?
How are kinetic parameters determined in enzyme kinetics studies?
What is one of the reasons for differentiating residues involved in catalysis from those involved in substrate binding?
What is one of the reasons for differentiating residues involved in catalysis from those involved in substrate binding?
Why is it important to understand the regulation of enzyme activity?
Why is it important to understand the regulation of enzyme activity?
What does the study of enzyme kinetics provide in terms of biocatalysis?
What does the study of enzyme kinetics provide in terms of biocatalysis?
What is the effect of increasing substrate concentration on the initial velocity of an enzymatic reaction?
What is the effect of increasing substrate concentration on the initial velocity of an enzymatic reaction?
Which enzyme relationship is represented by a hyperbolic curve when plotting initial velocity against substrate concentration?
Which enzyme relationship is represented by a hyperbolic curve when plotting initial velocity against substrate concentration?
What is the equation that explains the hyperbolic curve observed when plotting initial velocity versus substrate concentration?
What is the equation that explains the hyperbolic curve observed when plotting initial velocity versus substrate concentration?
What does steady state condition mean in enzyme kinetics?
What does steady state condition mean in enzyme kinetics?
Which assumptions allowed Michaelis and Menten to derive an equation fitting the hyperbolic curve in enzymatic reactions?
Which assumptions allowed Michaelis and Menten to derive an equation fitting the hyperbolic curve in enzymatic reactions?
In Michaelis-Menten kinetics, what does Km represent?
In Michaelis-Menten kinetics, what does Km represent?
What does Vmax represent in Michaelis-Menten kinetics?
What does Vmax represent in Michaelis-Menten kinetics?
Under steady-state conditions in enzyme kinetics, what does d[ES]/dT equal?
Under steady-state conditions in enzyme kinetics, what does d[ES]/dT equal?
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