Energy & Molecular Interactions Flashcards

1
Q

What is Energy?

A

ability to do work or cause change

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2
Q

What is Bioenergetics?

A

the study of energy in living organisms

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3
Q

What is Kinetic Energy?

A

energy of motion

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4
Q

What is Potential Energy?

A

stored energy

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5
Q

The First and Second Law of Thermodynamics

A

1st Law: Energy is neither created or destroyed. It is only transferrable or convertible.
2nd Law: The entropy of a system is increased. (hotter object to a cold object) –> to increase randomness and disorder

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6
Q

What is Gibbs Free Energy?

A

It’s “available” energy which is used to do work or capture chemical bonds

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7
Q

What variables affect Gibbs Free Energy?

A

Enthalpy (total energy of a closed system)
Entropy (order of system)
Temperature

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8
Q

Endergonic Reaction

A

it is a required investment of energy –> a non spontaneous reaction or anabolic –> Positive G

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9
Q

Exergonic Reaction

A

a release of energy –> a spontaneous reaction or catabolic –> Negative G

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10
Q

How does a catalyst increase the rate of a chemical reaction?

A

by lowering the activation energy

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11
Q

Ligand

A

A substrate (or small molecules that bind)

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12
Q

Substrate

A

a reactant

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13
Q

Define Induced Fit

A

When the active sites changes its shape for the substrates to fit/bind

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14
Q

What is Specificity?

A

when substrate(s) bind to a specific target
High Specificity: One other molecule
Low: Many other molecules

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15
Q

What is Affinity?

A

the tightness/measure of strength in which a substrate binds to an enzyme or other types of proteins
- the binding is reversible

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16
Q

What is Potency?

A

the amount of substrate needed to produce a certain effect.
- for example, EC50, can be used to compare the POTENCY of substrates that reach 50% of the maximum response better.

17
Q

What is Efficacy?

A

the capacity in which the response from a substrate can produce. (Maximum effect)

18
Q

What is Kd?

A

it is used to compare affinities

19
Q

What is Vmax?

A

The rate of product when enzyme become saturated by substrate

20
Q

What is EC50?

A

a concentration of substrate where enzyme reaches 50% Vmax.
- compares potency of substrate

21
Q

What is Saturation?

A

It is the point of no change in chemical reaction even after adding additional substrates.

22
Q

Define Competitive Antagonist

A

prevent AGONISTS from binding –> physically blocking the binding site

23
Q

Define Cofactor

A

metal ions –> help form the active site through a conformational change of the enzyme or help in enzyme-substrate binding.

24
Q

Define Coenzyme

A

organic molecules derived from water-soluble vitamins –> transport hydrogen atoms and other small molecules between enzymes

25
Q

Define Allosteric Antagonist

A

“inhibitors” that attach to the allosteric site of the enzyme/protein, and alter the shape of the binding site to NOT allow a substrate to bind to the enzyme.

26
Q

Define Allosteric Agonist

A

“activators” that attach to the allosteric site of the enzyme, and alter the active site for the substrate to fit and bind –> enhance function.

27
Q

How do cells regulate protein activity?

A
  • Temp. and pH
  • Concentration of cofactors, coenzymes, and enzymes
  • Covalent modification of the protein
  • Location of the enzyme
  • Allosteric Antagonists and allosteric agonists
28
Q

Define Phosphorylation

A
29
Q

Define Kinase

A

attach a phosphate to a protein

30
Q

Define dephosphorylation

A
31
Q

Define Phosphatase

A

remove a phosphate from a protein

32
Q

Define Proteolysis

A
33
Q

Explain how and why temperature and pH can affect protein function.

A

The optimal temperature is 37 degrees celcius
The optimal pH is 7.4
- Ex. immune system works better at a slightly higher temperature, if too much, protein denatures.
- ex. Digestive enzymes work best at differing pH, it can be reversible, but if it’s obscure, then it becomes irreversible

Prevents protein from denaturing