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
Define Allosteric Antagonist
"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
Define Allosteric Agonist
"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
How do cells regulate protein activity?
- Temp. and pH - Concentration of cofactors, coenzymes, and enzymes - Covalent modification of the protein - Location of the enzyme - Allosteric Antagonists and allosteric agonists
28
Define Phosphorylation
29
Define Kinase
attach a phosphate to a protein
30
Define dephosphorylation
31
Define Phosphatase
remove a phosphate from a protein
32
Define Proteolysis
33
Explain how and why temperature and pH can affect protein function.
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