Difference between revisions of "Bioblast quiz"
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= Exemplary quiz = | <!--= Exemplary quiz = | ||
:::: '''Note:''' Questions in this exemplary quiz were used from a set of questions prepared for the [[MiPschool Tromso-Bergen 2018]]: ''The protonmotive force and respiratory control. 1. Coupling of electron transfer reactions to vectorial translocation of protons. 2. From Einstein’s diffusion equation on gradients to Fick’s law on compartments.'' - [[Gnaiger 2018 MiPschool Tromso A2]] | :::: '''Note:''' Questions in this exemplary quiz were used from a set of questions prepared for the [[MiPschool Tromso-Bergen 2018]]: ''The protonmotive force and respiratory control. 1. Coupling of electron transfer reactions to vectorial translocation of protons. 2. From Einstein’s diffusion equation on gradients to Fick’s law on compartments.'' - [[Gnaiger 2018 MiPschool Tromso A2]] | ||
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</quiz> | </quiz> | ||
:{{purge | Reset Quiz}} | :{{purge | Reset Quiz}} --> | ||
= List of Quizzes on Bioblast = | = List of Quizzes on Bioblast = | ||
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{'''Which is NOT a parameter measured by integrating fluorometry into high-resolution respirometry?''' | {'''Which is NOT a parameter measured by integrating fluorometry into high-resolution respirometry?''' | ||
|type="()"} | |type="()"} | ||
- | - H<sub>2</sub>O<sub>2</sub> production | ||
|| | || H<sub>2</sub>O<sub>2</sub> production is measured. | ||
- O2 consumption rates | - O2 consumption rates | ||
|| Oxygen consumption is a primary measurement. | || Oxygen consumption is a primary measurement. | ||
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- Mitochondrial membrane potential changes | - Mitochondrial membrane potential changes | ||
|| Changes in membrane potential are indeed measured. | || Changes in membrane potential are indeed measured. | ||
| Line 183: | Line 144: | ||
{'''Which of the following is NOT a | {'''Which of the following is NOT a result of a measurement by the Oroboros-O2k?''' | ||
|type="()"} | |type="()"} | ||
- ATP production | - ATP production | ||
| Line 190: | Line 151: | ||
|| Calcium concentration is measured. | || Calcium concentration is measured. | ||
+ Protein synthesis rates | + Protein synthesis rates | ||
|| '''Correct!''' The Oroboros-O2k focuses on mitochondrial functionality such as ATP production, calcium concentration, and | || '''Correct!''' The Oroboros-O2k focuses on mitochondrial functionality such as ATP production, calcium concentration, and H<sub>2</sub>O<sub>2</sub> production, rather than protein synthesis. | ||
- | - H<sub>2</sub>O<sub>2</sub> production | ||
|| | || H<sub>2</sub>O<sub>2</sub> is within its capabilities. | ||
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{NADH-linked substrates are used in physiological respiratory states to: | {'''NADH-linked substrates are used in physiological respiratory states to:''' | ||
|type="()"} | |type="()"} | ||
- Reflect the exclusive type of substrates used by mitochondria | - Reflect the exclusive type of substrates used by mitochondria | ||
| Line 324: | Line 285: | ||
|| ROS production is a measurable parameter, indicative of oxidative stress. | || ROS production is a measurable parameter, indicative of oxidative stress. | ||
{'''The addition of fluorescent dyes in O2k- | {'''The addition of fluorescent dyes in Oroboros-O2k and NextGen-O2k measurements allows for the assessment of:''' | ||
|type="()"} | |type="()"} | ||
- Membrane fluidity and viscosity | - Membrane fluidity and viscosity | ||
| Line 376: | Line 337: | ||
|| Understanding the P/O ratio's implications on mitochondrial efficiency is crucial for assessing bioenergetic health. | || Understanding the P/O ratio's implications on mitochondrial efficiency is crucial for assessing bioenergetic health. | ||
{'''Assuming the standard reduction potential (E°') for NADH → NAD+ is -0.320 V and for | {'''Assuming the standard reduction potential (E°') for NADH → NAD<sup>+</sup> is -0.320 V and for O<sub>2</sub> → H<sub>2</sub>O is +0.815 V, calculate the ΔE°' for the electron transport from NADH to O<sub>2</sub>. What does ΔE°' indicate about the potential energy available for ATP synthesis?''' | ||
|type="()"} | |type="()"} | ||
+ ΔE°' = 1.135 V; indicates a high potential energy available for ATP synthesis | + ΔE°' = 1.135 V; indicates a high potential energy available for ATP synthesis | ||
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|| The calculation of ΔE°' provides | || The calculation of ΔE°' provides | ||
{'''If the inner mitochondrial membrane has a surface area of 5.0 × 10 | {'''If the inner mitochondrial membrane has a surface area of 5.0 × 10<sup>6</sup> μm<sup>2</sup> per mg of protein and each Complex I can pump 4 protons across the membrane, how many protons are pumped per second assuming a turnover number of 100 · s<sup>-1</sup> for Complex I?''' | ||
|type="()"} | |type="()"} | ||
- 2.0 | - 2.0 · 10<sup>9</sup> protons · s<sup>-1</sup> | ||
|| Without knowing the density of Complex I on the membrane, the calculation of protons pumped is speculative. | || Without knowing the density of Complex I on the membrane, the calculation of protons pumped is speculative. | ||
- 5.0 | - 5.0 · 10<sup>9</sup> protons · s<sup>-1</sup> | ||
|| Without knowing the density of Complex I on the membrane, the calculation of protons pumped is speculative. | || Without knowing the density of Complex I on the membrane, the calculation of protons pumped is speculative. | ||
- 2.0 | - 2.0 · 10<sup>9</sup> protons · s<sup>-1</sup> | ||
|| Without knowing the density of Complex I on the membrane, the calculation of protons pumped is speculative. | || Without knowing the density of Complex I on the membrane, the calculation of protons pumped is speculative. | ||
+ Calculation cannot be completed without the number of Complex I per μm | + Calculation cannot be completed without the number of Complex I per μm<sup>2</sup> | ||
|| '''Correct!''' This question tests the student's ability to identify key data points necessary for bioenergetic calculations, emphasizing the role of enzyme kinetics in mitochondrial function. | || '''Correct!''' This question tests the student's ability to identify key data points necessary for bioenergetic calculations, emphasizing the role of enzyme kinetics in mitochondrial function. | ||
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|| Precise calculation based on the given variables and constants illustrates a fundamental understanding of bioenergetic principles. | || Precise calculation based on the given variables and constants illustrates a fundamental understanding of bioenergetic principles. | ||
{'''The efficiency of mitochondrial oxidative phosphorylation can be described by the equation η = (ΔG_ATP/ΔG_O2) × 100%, where ΔG_ATP is the free energy change for ATP synthesis, and | {'''The efficiency of mitochondrial oxidative phosphorylation can be described by the equation η = (ΔG_ATP/ΔG_O2) × 100%, where ΔG_ATP is the free energy change for ATP synthesis, and ΔG_O<sub>2</sub> is the free energy change for oxygen reduction. If ΔG_ATP = -50 kJ/mol and ΔG_O<sub>2</sub> = -200 kJ/mol, what is the efficiency (η) of oxidative phosphorylation?''' | ||
|type="()"} | |type="()"} | ||
- 25% | - 25 % | ||
|| Accurately calculating η from the given free energy changes underscores the importance of efficiency in mitochondrial energy transformations. | || Accurately calculating η from the given free energy changes underscores the importance of efficiency in mitochondrial energy transformations. | ||
+ 50% | + 50 % | ||
|| '''Correct!''' This efficiency calculation provides a quantitative measure of how effectively mitochondria convert the energy from oxygen reduction into ATP synthesis, crucial for understanding metabolic energy conversion. | || '''Correct!''' This efficiency calculation provides a quantitative measure of how effectively mitochondria convert the energy from oxygen reduction into ATP synthesis, crucial for understanding metabolic energy conversion. | ||
- 75% | - 75 % | ||
|| Accurately calculating η from the given free energy changes underscores the importance of efficiency in mitochondrial energy transformations. | || Accurately calculating η from the given free energy changes underscores the importance of efficiency in mitochondrial energy transformations. | ||
- 100% | - 100 % | ||
|| Accurately calculating η from the given free energy changes underscores the importance of efficiency in mitochondrial energy transformations. | || Accurately calculating η from the given free energy changes underscores the importance of efficiency in mitochondrial energy transformations. | ||
{'''Consider a mitochondrial uncoupling scenario where the membrane potential (Δψ) is decreased by 50% without altering the proton gradient (ΔpH). Using the Nernst equation for protons, E = (RT/zF)ln([H+]out/[H+]in), predict how this change affects the pmF. Assume R, T, F, and z values remain constant.''' | {'''Consider a mitochondrial uncoupling scenario where the membrane potential (Δψ) is decreased by 50 % without altering the proton gradient (ΔpH). Using the Nernst equation for protons, E = (RT/zF)ln([H+]out/[H+]in), predict how this change affects the pmF. Assume R, T, F, and z values remain constant.''' | ||
|type="()"} | |type="()"} | ||
- pmF decreases by 50% | - pmF decreases by 50 % | ||
|| Understanding the composite nature of pmF and the logarithmic impact of changes in Δψ on pmF is crucial for interpreting the effects of mitochondrial uncoupling. | || Understanding the composite nature of pmF and the logarithmic impact of changes in Δψ on pmF is crucial for interpreting the effects of mitochondrial uncoupling. | ||
- pmF remains unchanged because ΔpH is constant | - pmF remains unchanged because ΔpH is constant | ||
|| Understanding the composite nature of pmF and the logarithmic impact of changes in Δψ on pmF is crucial for interpreting the effects of mitochondrial uncoupling. | || Understanding the composite nature of pmF and the logarithmic impact of changes in Δψ on pmF is crucial for interpreting the effects of mitochondrial uncoupling. | ||
+ pmF decreases, but not by 50% | + pmF decreases, but not by 50 % | ||
|| '''Correct!''' The pmF is affected by both Δψ and ΔpH. A decrease in Δψ reduces pmF, but the extent is not directly proportional due to the logarithmic relationship in the Nernst equation. | || '''Correct!''' The pmF is affected by both Δψ and ΔpH. A decrease in Δψ reduces pmF, but the extent is not directly proportional due to the logarithmic relationship in the Nernst equation. | ||
- Cannot predict without specific [H+]out/[H+]in values | - Cannot predict without specific [H+]out/[H+]in values | ||
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:{{purge | Reset Quiz}} | :{{purge | Reset Quiz}} | ||
=== Chapter 1.2 specific questions === | === Chapter 1.2 specific questions === | ||
Latest revision as of 12:10, 12 April 2024
Self educational quizzes
The Bioblast quiz has been initiated by Ondrej Sobotka.
- For tips&tricks and detailed instructions about how to make a quiz visit links below:
List of Quizzes on Bioblast
- Please link your quizzes to this page and feel free to contribute!
Blue Book Bioblast Quiz
Blue Book chapter 1: basic questions
Blue Book chapter 1: Advanced questions
Chapter 1.2 specific questions
