Lecture 1 Flashcards

1
Q

What is the definition of energy?

A

The capacity to do work.

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2
Q

What is the difference between kinetic and potential energy?

A

Kinetic: using energy to do something → energy of motion
Ex. breaking chemical bond releases energy
Potential energy: storing energy for later
Ex. creating bonds to do so

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3
Q

______________ occurs when energy is transferred from one molecule to another and are used in many different biological processes. Fill in the blank.

A

Redox Reactions

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4
Q

What is the difference between oxidation and reduction processes?

A

oxidation →loss of electrons vs. reduction → gaining electrons

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5
Q

______________ is the ability of organisms to store energy in molecules by transferring electrons (i.e. energy) to them. Fill in the blank.

A

Reducing power

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6
Q

Which statement describes any information discussed in class regarding the First Law of Thermodynamics?

A
  • The First Law of Thermodynamics (FLOT):Energy cannot be created nor destroyed, it can only change from one form to another

Ex. When we eat, the food get broken down, we are changing the form of it and removing the energy stored within the glucose molecules
Ex2.or when something goes from potential to kinetic energy
Ex3. Lion consumes a giraffe eats it for energy, plant uses light energy and carbon to create glucose molecules (we cannot do this)
Energy before → energy after (whatever you put in you get out)

  • Chemical potential energy in the body can convert into other form and some of the energy dissipates into environment as heat
    The FLOT energy cannot be created or destroyed but doesn’t mean it cannot be transformed into something else and heat is typically a byproduct which is technically still considered to be a part of that energy
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7
Q

What is often a byproduct of a chemical reaction (according to the First Law of Thermodynamics)?

A

Heat

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8
Q

Which statement describes any information discussed in class regarding the Second Law of Thermodynamics?

A

The Second Law of Thermodynamics (SLOT): This concerns the transformation of potential energy into heat or random molecular motion, a disorder referred to as entropy.
The universe is continuously increasing, disorder is more likely than order
When one consumes food we don’t use every single tiny bit, like the cellulose in plant, it’s unusable energy or waste material, so disorder is more likely than order, the chances of eating something and utilizing every minute molecule is not possible reason for urine and feces, you will also release heat also considered waste

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9
Q

What is the definition of either (a) entropy, (b) or free energy?

A

Entropy: The measure of disorder in a system
Free Energy: So H can be the one you intake food depending on body process you have to subtract how much energy it takes to break down that food and the leftover is free energy utilize of everyday activities or create adipose tissue or fat in the body, extra used for other process

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10
Q

What is the equation for Gibbs free energy?

A

G = H – TS

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11
Q

What does each letter represent (the word and what it means) within the equation for Gibbs free energy?

A

Gibbs Free Energy Equation: The amount of energy available to break and subsequently form other chemical bonds, energy available to do work
H- enthalpy (energy contained in a molecules chemical bonds)
T- when ones consumes food, they need to subtract the heat energy and the temperature they’re dealing with
Entropy (S)- energy unavailable cause of disorder
When H is subtracted from TH, this tells one Gibbs Free Energy, the amount available to actually do something in the body

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12
Q

What is the difference between an endergonic and exergonic reaction?

A

Endergonic: reaction that requires input of energy (called “plus G”)
Exergonic: if you want to release energy and you go from a reactant to a product, any reaction that requires the release of excess energy in terms of heat is exergonic (called “negative G”)

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13
Q

What is the definition of activation energy?

A

Activation Energy: The energy required to destabilize existing chemical bonds and initiate a chemical bonds, energy needed to start a reaction

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14
Q

How are catalysts useful for completing chemical reactions?

A

If one uses catalyst, reaction activation energy needed is lessened, something not using a catalyst require more activation energy to begin a chemical reaction

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15
Q

Which statement does not describe the structure of ATP?

A

ATP (ademine triphosphate) is a nucleotide with three smaller components: Ribose, adenine nitrogen group, triphosphate group, its main component of monomer is nucleotide
The statment above describes the components of ATP. Anything that controdicts the statment would be correct in the context of the question.

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16
Q

How does ATP store and release energy (know the specific bond we discussed)?

A

ATP stores energy in the bonds between the phosphate groups which have a low activation energy to be broken, can release a lot on energy when broken
Turns from ATP → breaks of phosphate a becomes ADP (Adenine diphosphate) → add phosphate group to build up energy again.

17
Q

What is the difference between the structures of ATP and ADP (there is only one main difference we discussed in class)?

A

ATP has an extra phosphate group while ADP only has 2.
Hint: ATP (T- Triphosphate) vs. ADP (Diphosphate)
Tri: means 3 and Di: means 2

18
Q

Cells use proteins called ___________ as catalysts to lower activation energy during chemical reactions. Fill in the blank.

A

enzymes

19
Q

What is a substrate?

A

Will attach to the active site of the enzyme, it’ll hold it, enclose upon it, change it and then once released it’ll be a completely different component, in simple terms it’s the molecule

20
Q

What is the definition of the active site of an enzyme?

A

Active Site: where it’s actively accepting something to go and do a reaction. It’s usually where the substrate binds to the enzymes, a specific area (pocket or cleft in enzyme)

21
Q

What is the definition of an enzyme-substrate complex?

A

When the substrate and enzyme are connected and different chemical process take place inside the area, substrate will bind to the actual enzyme and it’ll be the active site and then undergo a chemical reaction

22
Q

What is the definition of a multienzyme?

A

Multienzyme Complexes: When several enzymes catalyze different steps of a sequence of reaction and are associated with one another in non-covalent bonding assemblies
Explained: you don’t just have enzyme and substrate attaching, multiple reactions might need to occur in order to actually do something

23
Q

Which is not an advantage of using multienzymes verses regular enzymes?

A

There are 3 main advantages: The statement above describes the components of ATP. Anything that contradicts the statement would be correct in the context of the question.

a. Rate of any enzyme is limited by how often the enzyme collides with a substance, so it’ll collide much faster if it’s right next to another enzyme.

b. Reacting substance does not leave the complex while it goes through a series of reactions, so side reactions are not possible.

c. All of the reactions that take place in the MEC can be controlled as a unit, chances of something going wrong is minimal.

24
Q

________ are chemical components which assist in an enzyme’s function. ________ are when the cofactor is a non-protein organic molecules (i.e. vitamins). Fill in the blanks.

A
  1. Cofactors
  2. Coenzyme
25
Q

For specific enzymes, what happens when a cofactor is not attached to its designed enzyme?

A

Remember just became we have the enzymes doesn’t mean they can carry out process all on their own, vitamin are big example of coenzymes because they get a chemical process going

26
Q

Which statement explains how temperature and pH can affect enzymes?

A

Temperature: increase temp. → increase rate of reaction

Normally all different types of temperatures each enzyme can function at, different optimal operating temperatures for each enzyme
PH: as pH value is increased above or decreased below the optimum pH the enzyme activity decreases

27
Q

What is the definition of an enzymatic inhibitor?

A

substance that bind to enzyme and decrease activity

28
Q

What is the difference between a competitive inhibitor and noncompetitive inhibitor?

A

Competitive Inhibitor: If inhibitor attaches to active site, because it competes with substrate for the same active site displacing a percentage of substrate molecules from the enzyme

Noncompetitive Inhibitor: The allosteric inhibitor changes of shape of enzyme so it cannot bind to substrate, turns it off

29
Q

What is the definition of an allosteric site of an enzyme?

A

chemical on or off switch that some enzymes have, if nothing is in it then you are perfectly fine, can work for or against it, if inhibitor is attached you cannot complete any type of chemical reaction or enzyme substrate reaction

30
Q

What is the definition of either an (a) allosteric inhibitor or (b) allosteric activator?

A

Allosteric inhibitors modify the active site of the enzyme so that substrate binding is reduced or prevented. In contrast, allosteric activators modify the active site of the enzyme so that the affinity for the substrate increases.

31
Q

What is the definition of a biochemical pathway?

A

Any type of reaction that involves enzymes, the product of one reaction becomes the substrate to the next reactant

32
Q

What is the definition of metabolism?

A

total of all chemical reactions carried out by organisms, only two process (make or break)

33
Q

What is the difference between the metabolic processes of catabolism and anabolism?
Anabolism: type of reaction that expends energy to make or transform chemical bonds
Ex. During photosynthesis form and make glucose in a simple product
Catabolism: reactions that harvest energy when chemical bond are broken
Ex. We do this when we eat food, break it down for energy, cellular respiration

A

Anabolism: type of reaction that expends energy to make or transform chemical bonds
Ex. During photosynthesis form and make glucose in a simple product

Catabolism: reactions that harvest energy when chemical bond are broken
Ex. We do this when we eat food, break it down for energy, cellular respiration

34
Q

Many different biochemical pathways regulate their metabolic processes by using feedback inhibition pathways. What is the definition of feedback inhibition?

Feedback inhibition: biochemical pathway in which the final product becomes the allosteric inhibitor for the first enzyme in the pathway
Why?: When there are too many it eventually has to stop

A

Feedback inhibition: biochemical pathway in which the final product becomes the allosteric inhibitor for the first enzyme in the pathway

Why?: When there are too many it eventually has to stop