Bio thermodynamics Flashcards

(25 cards)

1
Q

What determines chemical reactions and energy?

A

The concentration of reactants and products.

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2
Q

What are the two types of metabolic reactions?

A

Anabolic and catabolic.

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3
Q

What is an anabolic reaction?

A

Small molecules assemble to form a larger molecule.

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4
Q

What is a catabolic reaction?

A

Large molecules are broken into smaller molecules.

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5
Q

What are the two types of energy changes in reactions?

A

Exergonic and endergonic.

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6
Q

What is an exergonic reaction?

A

Free energy is released (spontaneous with -ΔG).

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7
Q

What is an endergonic reaction?

A

Free energy is absorbed (nonspontaneous with +ΔG).

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8
Q

What is the role of enzymes in reactions?

A

Enzymes act as catalysts by lowering the activation energy needed for a reaction.

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9
Q

What are most enzymes made of?

A

Most are proteins, but some are made of RNA (ribozymes).

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10
Q

What is the active site of an enzyme?

A

The area of the enzyme where the substrate binds.

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11
Q

What is an allosteric site?

A

A secondary location where an effector binds (effectors can be activators or inhibitors).

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12
Q

What happens when substrates enter the active site?

A

Enzyme and substrate change shape slightly to better catalyze the reaction (induced fit model).

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13
Q

What is the enzyme-substrate complex?

A

Formed when the substrate binds the enzyme.

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14
Q

What are the characteristics of enzyme function?

A

Substrate specific, unchanged by the reaction, catalyze forward and reverse reactions, vary depending on pH and temperature, and have an active site that binds substrates via induced fit.

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15
Q

What is competitive inhibition?

A

A substance that mimics the substrate inhibits the enzyme by binding to the active site, preventing substrate binding.

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16
Q

How can competitive inhibition be overcome?

A

By increasing substrate concentration.

17
Q

What happens to Km and Vmax in competitive inhibition?

A

Km increases and Vmax stays the same.

18
Q

What is noncompetitive inhibition?

A

A substance inhibits the enzyme by binding to the allosteric site, preventing the reaction.

19
Q

What happens to Km and Vmax in noncompetitive inhibition?

A

Km stays the same and Vmax decreases.

20
Q

What is ATP?

A

A source of chemical energy formed via phosphorylation, creating energy-rich triphosphate bonds.

21
Q

What is ATP hydrolysis?

A

Broken apart via hydrolysis, releasing energy and phosphate.

22
Q

What is the difference between potential and kinetic energy?

A

Kinetic energy is energy in motion (i.e., jumping), while potential energy is stored energy (i.e., glycogen).

23
Q

What is Vmax?

A

The maximum velocity of the reaction at peak substrate saturation.

24
Q

What is the Michaelis Constant (Km)?

A

The substrate concentration at which the rate of the reaction is half of the maximum velocity.

25
What does a small Km indicate?
Less substrate is needed to reach Vmax (i.e., higher binding affinity).