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05.05.202521:53
important terms in physics for EUEE
1. Force: An interaction that causes an object to change its velocity, typically measured in newtons (N).
2. Mass: A measure of the amount of matter in an object, usually measured in kilograms (kg).
3. Weight: The force exerted by gravity on an object, calculated as the mass of the object multiplied by the acceleration due to gravity (W = mg).
4. Energy: The capacity to do work, which can exist in various forms such as kinetic, potential, thermal, and chemical energy.
5. Kinetic Energy: The energy possessed by an object due to its motion, calculated using the formula KE = 1/2 mv^2, where m is mass and v is velocity.
6. Potential Energy: The energy stored in an object due to its position or configuration, often associated with gravitational or elastic forces.
7. Work: The energy transferred to or from an object via the application of force along a displacement, calculated as W = Fd cos(θ), where F is force, d is displacement, and θ is the angle between the force and displacement vectors.
8. Power: The rate at which work is done or energy is transferred, measured in watts (W), where 1 W = 1 J/s.
9. Momentum: The quantity of motion an object has, defined as the product of its mass and velocity (p = mv).
10. Impulse: The change in momentum of an object when a force is applied over a period of time, calculated as J = F Δ t.
11. Acceleration: The rate of change of velocity of an object with respect to time, measured in meters per second squared (m/s²).
12. Newton’s Laws of Motion: Three fundamental principles that describe the relationship between the motion of an object and the forces acting on it:
- First Law: An object at rest stays at rest, and an object in motion stays in motion unless acted upon by a net external force.
- Second Law: The acceleration of an object is directly proportional to the net force acting on it and inversely proportional to its mass (F = ma).
- Third Law: For every action, there is an equal and opposite reaction.
13. Friction: The resistance encountered when one surface moves over another, which can be static or kinetic.
14. Thermodynamics: The branch of physics that deals with heat, work, temperature, and energy transfer.
15. Entropy: A measure of disorder or randomness in a system; in thermodynamics, it indicates the direction of spontaneous processes.
16. Electric Charge: A property of matter that causes it to experience a force in an electromagnetic field; charges can be positive or negative.
17. Voltage: The electric potential difference between two points in a circuit, measured in volts (V).
18. Current: The flow of electric charge in a circuit, measured in amperes (A).
19. Resistance: The opposition to the flow of electric current in a conductor, measured in ohms (Ω).
20. Ohm’s Law: A fundamental relationship in electrical circuits stating that V = IR, where V is voltage, I is current, and R is resistance.
21. Wave: A disturbance that transfers energy through space or matter, characterized by its wavelength, frequency, and amplitude.
22. Frequency: The number of cycles of a wave that pass a given point per unit time, measured in hertz (Hz).
23. Wavelength: The distance between successive crests (or troughs) of a wave, typically measured in meters.
24. Refraction: The bending of light as it passes from one medium to another due to a change in speed.
25. Reflection: The bouncing back of light or sound waves when they encounter a surface.
26. Gravity: A natural phenomenon by which all things with mass are attracted toward one another; described by Newton’s law of universal gravitation.
27. Quantum Mechanics: The branch of physics that deals with the behavior of particles on very small scales, such as atoms and subatomic particles.
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05.05.202518:52
19. In the Lock and Key Model, the enzyme's active site:
A. Is flexible and adjusts to accommodate the substrate.
B. Has a rigid, specific shape that matches only one substrate.
C. Undergoes major changes when the substrate binds.
D. Is adapted to catalyze multiple types of reactions.
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A. Is flexible and adjusts to accommodate the substrate.
B. Has a rigid, specific shape that matches only one substrate.
C. Undergoes major changes when the substrate binds.
D. Is adapted to catalyze multiple types of reactions.
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05.05.202518:39
15. Which of the following best describes the relationship between enzyme activity and temperature?
A. Enzyme activity always increases with temperature.
B. Enzyme activity is not affected by temperature.
C. Enzyme activity increases with temperature until an optimal point, after which it declines due to denaturation.
D. Enzyme activity decreases as temperature decreases but never reaches zero.
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A. Enzyme activity always increases with temperature.
B. Enzyme activity is not affected by temperature.
C. Enzyme activity increases with temperature until an optimal point, after which it declines due to denaturation.
D. Enzyme activity decreases as temperature decreases but never reaches zero.
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05.05.202518:27
11. What is the effect of a competitive inhibitor on enzyme activity?
A. It binds to the active site, preventing the substrate from binding.
B. It increases the rate of reaction by binding to the enzyme.
C. It binds to a site other than the active site, changing the enzyme's shape.
D. It has no effect on enzyme activity.
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A. It binds to the active site, preventing the substrate from binding.
B. It increases the rate of reaction by binding to the enzyme.
C. It binds to a site other than the active site, changing the enzyme's shape.
D. It has no effect on enzyme activity.
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05.05.202518:18
6. Why is enzyme kinetics important in drug design?
A. It helps determine the molecular weight of enzymes
B. It explains why all enzymes are proteins
C. It allows the prediction of how inhibitors affect enzyme activity
D. It shows that enzymes are not reusable
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A. It helps determine the molecular weight of enzymes
B. It explains why all enzymes are proteins
C. It allows the prediction of how inhibitors affect enzyme activity
D. It shows that enzymes are not reusable
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05.05.202518:03
2, What is the primary difference between competitive and non-competitive inhibitors in enzyme activity?
A. Competitive inhibitors bind to the enzyme's active site, while non-competitive inhibitors bind to a different site.
B. Competitive inhibitors bind to the enzyme's allosteric site, while non-competitive inhibitors bind to the active site.
C. Competitive inhibitors increase enzyme activity, while non-competitive inhibitors decrease it.
D. Competitive inhibitors do not affect the reaction rate, while non-competitive inhibitors increase it.
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A. Competitive inhibitors bind to the enzyme's active site, while non-competitive inhibitors bind to a different site.
B. Competitive inhibitors bind to the enzyme's allosteric site, while non-competitive inhibitors bind to the active site.
C. Competitive inhibitors increase enzyme activity, while non-competitive inhibitors decrease it.
D. Competitive inhibitors do not affect the reaction rate, while non-competitive inhibitors increase it.
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05.05.202519:07
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05.05.202518:48
18. According to the Induced Fit Model, what happens when the substrate binds to the enzyme's active site?
A. The enzyme and substrate fit together perfectly without any changes.
B. The active site of the enzyme undergoes a slight change to fit the substrate.
C. The substrate remains unchanged, and the enzyme's active site remains rigid.
D. The substrate binds at multiple sites on the enzyme.
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A. The enzyme and substrate fit together perfectly without any changes.
B. The active site of the enzyme undergoes a slight change to fit the substrate.
C. The substrate remains unchanged, and the enzyme's active site remains rigid.
D. The substrate binds at multiple sites on the enzyme.
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05.05.202518:37
14. Which of the following can increase the rate of an enzyme-catalyzed reaction?
A. Decreasing enzyme concentration
B. Increasing the concentration of the product
C. Increasing substrate concentration up to a certain point
D. Decreasing pH to a level lower than the enzyme’s optimal range
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A. Decreasing enzyme concentration
B. Increasing the concentration of the product
C. Increasing substrate concentration up to a certain point
D. Decreasing pH to a level lower than the enzyme’s optimal range
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05.05.202518:24
10. What happens to an enzyme if the pH is too high or too low compared to its optimal pH?
A. The enzyme becomes more efficient.
B. The enzyme activity remains unaffected.
C. The enzyme may denature and lose its ability to function.
D. The enzyme changes shape and becomes more active.
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A. The enzyme becomes more efficient.
B. The enzyme activity remains unaffected.
C. The enzyme may denature and lose its ability to function.
D. The enzyme changes shape and becomes more active.
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05.05.202518:12
5, What would you observe on a graph of reaction rate versus substrate concentration when a non competitive inhibitor is present?
A. The graph will show a higher Vmax but the same Km.
B. The graph will show a lower Vmax and the same Km.
C. The graph will show the same Vmax but a higher Km.
D. The graph will show a higher Vmax and a lower Km.
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A. The graph will show a higher Vmax but the same Km.
B. The graph will show a lower Vmax and the same Km.
C. The graph will show the same Vmax but a higher Km.
D. The graph will show a higher Vmax and a lower Km.
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05.05.202518:00
1, Which of the following represents the correct interpretation of the graph for letter a, b and c respectively?
A. Competitive inhibitor, no inhibitors and non-competitive inhibitors
B. Noncompetitive inhibitor, competitive inhibitor and no inhibitors
C. No inhibitors, competitive inhibitors and non-competitive inhibitors
D. No inhibitors, non-competitive inhibitors and competitive inhibitors
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A. Competitive inhibitor, no inhibitors and non-competitive inhibitors
B. Noncompetitive inhibitor, competitive inhibitor and no inhibitors
C. No inhibitors, competitive inhibitors and non-competitive inhibitors
D. No inhibitors, non-competitive inhibitors and competitive inhibitors
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05.05.202519:02
✅ Full Answer For Today Questions | Enzyme |
1. C. No inhibitors, competitive inhibitors and non-competitive inhibitors.
2. A. Competitive inhibitors bind to the enzyme's active site, while non-competitive inhibitors bind to a different site.
3. C. The reaction rate decreases, but increasing substrate concentration can overcome the effect.
4. C. The graph for the inhibitor will show a lower Vmax but the same initial rate.
5. B. The graph will show a lower Vmax and the same Km.
6. C. It allows the prediction of how inhibitors affect enzyme activity.
7. B. Modify the enzyme’s active site for better substrate binding at low energy states.
8. C. It allows the prediction of how inhibitors affect enzyme activity.
9. B. It can increase enzyme activity up to an optimal temperature, after which the activity decreases.
10. C. The enzyme may denature and lose its ability to function.
11. A. It binds to the active site, preventing the substrate from binding.
12. A. Increasing enzyme concentration increases the reaction rate until all substrates are used up.
13. C. It binds to a site other than the active site, causing the enzyme to change shape and reducing its activity.
14. C. Increasing substrate concentration up to a certain point.
15. C. Enzyme activity increases with temperature until an optimal point, after which it declines due to denaturation.
16. D. The wavelength of light used during the reaction.
17. B. The enzyme has a rigid active site that fits exactly with the substrate.
18. B. The active site of the enzyme undergoes a slight change to fit the substrate.
19. B. Has a rigid, specific shape that matches only one substrate.
20. A. A hand fitting into a glove.
1. C. No inhibitors, competitive inhibitors and non-competitive inhibitors.
2. A. Competitive inhibitors bind to the enzyme's active site, while non-competitive inhibitors bind to a different site.
3. C. The reaction rate decreases, but increasing substrate concentration can overcome the effect.
4. C. The graph for the inhibitor will show a lower Vmax but the same initial rate.
5. B. The graph will show a lower Vmax and the same Km.
6. C. It allows the prediction of how inhibitors affect enzyme activity.
7. B. Modify the enzyme’s active site for better substrate binding at low energy states.
8. C. It allows the prediction of how inhibitors affect enzyme activity.
9. B. It can increase enzyme activity up to an optimal temperature, after which the activity decreases.
10. C. The enzyme may denature and lose its ability to function.
11. A. It binds to the active site, preventing the substrate from binding.
12. A. Increasing enzyme concentration increases the reaction rate until all substrates are used up.
13. C. It binds to a site other than the active site, causing the enzyme to change shape and reducing its activity.
14. C. Increasing substrate concentration up to a certain point.
15. C. Enzyme activity increases with temperature until an optimal point, after which it declines due to denaturation.
16. D. The wavelength of light used during the reaction.
17. B. The enzyme has a rigid active site that fits exactly with the substrate.
18. B. The active site of the enzyme undergoes a slight change to fit the substrate.
19. B. Has a rigid, specific shape that matches only one substrate.
20. A. A hand fitting into a glove.
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05.05.202518:47
17. Which of the following best describes the Lock and Key Model of enzyme action?
A. The enzyme's active site undergoes a conformational change when the substrate binds.
B. The enzyme has a rigid active site that fits exactly with the substrate.
C. The enzyme's active site is flexible and adapts to fit the substrate.
D. The substrate changes shape to fit the enzyme's active site.
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A. The enzyme's active site undergoes a conformational change when the substrate binds.
B. The enzyme has a rigid active site that fits exactly with the substrate.
C. The enzyme's active site is flexible and adapts to fit the substrate.
D. The substrate changes shape to fit the enzyme's active site.
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05.05.202518:33
13. What is a non-competitive inhibitor’s effect on enzyme activity?
A. It competes with the substrate for the active site.
B. It binds to the active site, preventing the substrate from binding.
C. It binds to a site other than the active site, causing the enzyme to change shape and reducing its activity.
D. It accelerates the reaction rate by increasing substrate binding.
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A. It competes with the substrate for the active site.
B. It binds to the active site, preventing the substrate from binding.
C. It binds to a site other than the active site, causing the enzyme to change shape and reducing its activity.
D. It accelerates the reaction rate by increasing substrate binding.
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05.05.202518:23
9. How does an increase in temperature typically affect enzyme activity?
A. It always increases enzyme activity.
B. It can increase enzyme activity up to an optimal temperature, after which the activity
decreases.
C. It decreases enzyme activity consistently.
D. Temperature has no effect on enzyme activity.
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A. It always increases enzyme activity.
B. It can increase enzyme activity up to an optimal temperature, after which the activity
decreases.
C. It decreases enzyme activity consistently.
D. Temperature has no effect on enzyme activity.
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05.05.202518:09
4, If you were graphing the reaction rate versus substrate concentration for a reaction with a competitive inhibitor, what would you expect the graph to look like compared to the control (no inhibitor)?
A. The graph for the inhibitor will show a steeper slope and reach Vmax faster.
B. The graph for the inhibitor will show a higher Vmax but a lower initial rate.
C. The graph for the inhibitor will show a lower Vmax but the same initial rate.
D. The graph for the inhibitor will show the same Vmax but a higher initial rate.
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A. The graph for the inhibitor will show a steeper slope and reach Vmax faster.
B. The graph for the inhibitor will show a higher Vmax but a lower initial rate.
C. The graph for the inhibitor will show a lower Vmax but the same initial rate.
D. The graph for the inhibitor will show the same Vmax but a higher initial rate.
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05.05.202513:10
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05.05.202518:54
20. The Lock and Key Model of enzyme action can be compared to:
A. A hand fitting into a glove
B. A lock opening with a key of any shape.
C. A key that changes shape to fit any lock.
D. A hand changing its shape to fit any glove.
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A. A hand fitting into a glove
B. A lock opening with a key of any shape.
C. A key that changes shape to fit any lock.
D. A hand changing its shape to fit any glove.
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05.05.202518:43
16. Which factor does NOT typically affect enzyme-catalyzed reactions?
A. Ionic strength of the environment
B. The concentration of the substrate and enzyme
C. The presence of coenzymes or cofactors
D. The wavelength of light used during the reaction
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A. Ionic strength of the environment
B. The concentration of the substrate and enzyme
C. The presence of coenzymes or cofactors
D. The wavelength of light used during the reaction
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05.05.202518:32
12. How does enzyme concentration influence enzyme activity?
A. Increasing enzyme concentration increases the reaction rate until all substrates are used up.
B. Enzyme concentration has no effect on the reaction rate.
C. Increasing enzyme concentration decreases the reaction rate.
D. Enzyme concentration decreases the activity of enzymes.
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A. Increasing enzyme concentration increases the reaction rate until all substrates are used up.
B. Enzyme concentration has no effect on the reaction rate.
C. Increasing enzyme concentration decreases the reaction rate.
D. Enzyme concentration decreases the activity of enzymes.
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05.05.202518:18
7. If you were designing an enzyme to work efficiently at low temperatures, which factor would you modify?
A. Increase the enzyme’s Km
B. Modify the enzyme’s active site for better substrate binding at low energy states
C. Increase the enzyme’s denaturation temperature
D. Remove all cofactors
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A. Increase the enzyme’s Km
B. Modify the enzyme’s active site for better substrate binding at low energy states
C. Increase the enzyme’s denaturation temperature
D. Remove all cofactors
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05.05.202518:08
3, What happens to the reaction rate when a competitive inhibitor is added to the enzyme-substrate reaction?
A. The reaction rate decreases at all substrate concentrations.
B. The reaction rate increases, and the enzyme becomes more efficient.
C. The reaction rate decreases, but increasing substrate concentration can overcome the effect.
D. The reaction rate is unaffected by substrate concentration.
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A. The reaction rate decreases at all substrate concentrations.
B. The reaction rate increases, and the enzyme becomes more efficient.
C. The reaction rate decreases, but increasing substrate concentration can overcome the effect.
D. The reaction rate is unaffected by substrate concentration.
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05.05.202506:36
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