Unit 2: Enegy And Enzmes Structure And Funtction Flashcards

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0
Q

Kinetic energy

A

Energy of motion

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1
Q

Energy

A

Capacity to perform work(change/rearrange matter)

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2
Q

Heat energy

A

Movement of molecules or atoms in a body of matter

Most disordered form of energy

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3
Q

Potential energy

A

Stored energy that an object possess as a result of it’s location or structure

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4
Q

Chemical energy

A

The potential energy of molecules

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5
Q

The first law of thermodynamics

A

(Law of conservation of energy)

Energy cannot be created nor destroyed but can change forms and be transferred

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6
Q

The second law of thermodynamics

A

*every process in the universe leads toward a higher disorder *
Orderly(low entropy) arrangements take energy investment

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7
Q

Entropy

A

The measure of disorder

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8
Q

Higher entropy, _____ disorder

A

Higher

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9
Q

Exergonic reactions

A

Chemical reactions that release energy, because reactants have more energy than products.
A+B —> C + energy

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10
Q

Examples of exergonic reactions

A

Digesting food
Burning coal, wood
Hydrolysis

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11
Q

Endergonic reactions

A

Chemical reactions that take in energy, because reactants have less energy than products.
A + B + energy —> C

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12
Q

Examples of endergonic reactions

A

Dehydration synthesis
Freezing
Photosynthesis

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13
Q

ATP

A

Adenosine Triphosphate Structure and Function.
A molecule that is used to directly fuel chemical reactions with small portions of energy.
ATP breaks down a (P) to provide energy.
The (P) binds to another molecule and activates to do cellular works.
^^phosphorylation
ADP can bind with (P) in endergonic reactions to form new ATP molecules.

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14
Q

Activation energy

A

The energy required to start a chemical reaction.
This energizes the reactants.
Living organisms use enzymes as proteins that lower the activation energy of a reaction so reactions can take place within a measurable time.

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15
Q

Enzymes function

A

A protein that lowers the activation energy of a reaction so reactions can take place within measurable time

16
Q

Structure of enzyme

A

Has an active site(binds with substrates, competitive inhibitors) and an allosteric site(binds with noncompetitive inhibitors).

17
Q

Active site

A

Part of the enzyme that binds with the reactant.

Changes shape during i ding and forces the substrates to have an induced fit.

18
Q

Allosteric site

A

Noncompetitive inhibitors bind with Allosteric site

19
Q

Enzymes

A

Enzyme catalyze reactions by binding with substrates. Part of the enzyme that’s binds with the reactant is the active site. The active site changes its shape during binding and forces the substrate to react<— induced fit. Enzymes are very specific and only bind with one toe of substrate(s). Once the reaction is completed the product is released and the enzyme is used again.

20
Q

enzymes are proteins….

A

Because enzymes are proteins they are sensitive to their environment. They function best at optimal pH, temperature, and salt concentration
^6-8. ^95-104F. ^not tosalty solutions

21
Q

Temperature

A

Above higher than optimal temperature enzymes slow down, then denature and don’t function any more. Below the optimal temperature enzymes also slow down but don’t denature.

22
Q

pH

A

Kenzie’s function best at their optimal pH. If the pH gets higher or lower they slow down then denature.

23
Q

Inhibitors

A

Substances that can bind to the enzyme and slow it down or stop the enzyme from functioning.

24
Q

Competitive inhibitors

A

Bind to active site

25
Q

Noncompetitive inhibitors

A

Bind to Allosteric site

26
Q

Toxins

A

Can be inhibitors that perms fly bind to the enzyme and destroy it.