Proteins, Lipids, Carbs and Enzymes Flashcards

1
Q

What is feedback inhibition?

A

When the product of a pathway prevents too much build of the product

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2
Q

Why is feedback inhibition important?

A

It provides a means of self-regulating the system.

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3
Q

What type of regulation control the conversation of threonine to isoleucine?

A

allosertic regulation. The final product of this reaction threonine is an allosteric inhibitor of the first enzyme.

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4
Q

Does the threonine deaminase have both an active and an allosteric site?

A

Yes, it does. The active site is where the substrate threonine binds. The allosteric site is where isoleucine binds to performs feedback inhibition

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5
Q

What are the two ways energy is created in a cell?

A
  1. ) Transfer of high energy electrons

2. ) Transfer of a phosphate group

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6
Q

What happens when a molecule loses an electron?

A

Oxidation

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7
Q

What happens when a molecule gains an electron?

A

reduction

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8
Q

Oxidation is endergonic or exergonic?

A

When something is oxidized the reaction that has occurred is exergonic

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9
Q

Is reduction endergonic of exergonic?

A

When somethings is reduced the reaction that had occurred is endergonic

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10
Q

What is the formula for glucose?

A

C6H12O6

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11
Q

Is ATP like rna or dna?

A

It is like DNA because of the OH on both point of the ribose

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12
Q

What is phosphorylation?

A

The addition of a phosphate group to a substate during to drive endergonic reactions.

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13
Q

What would causes irreversible changes to an enzyme?

A

They are often the result of changes to the protein’s primary structure.

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14
Q

What does pH alter the secondary and tertiary?

A

Changes in pH alter the hydrogen bonds.

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15
Q

How do polymers form?

A

Via condensation

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16
Q

How do polymers break apart?

A

Via hydrolysis

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17
Q

What is the shape of saccharides?

A

A linear ring formation

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18
Q

What stabilizes the secondary structure of proteins?

A

Polar interactions between the back bone. The R groups are not involved.

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19
Q

What stabilizes the tertiary structures of the protein?

A

interactions between the R groups. This is often called the 3-D protein

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20
Q

What bonds the quaternary structure of proteins?

A

relationship among the polypeptide chains are stabilized by r-group interactions, h bonds, ionic interactions

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21
Q

What must proteins have in order to have a quaternary structure?

A

More than one subunit

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22
Q

What is a peptide bond and why does it matter?

A

Holds the backbone of amino acids together.

peptide bond is a chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O). This is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids.

23
Q

What causes protein to denature?

A

Changes in environment and chemical interactions can alter protein shape.

Often a non-permanent change. Not at the primary level. It is al alteration in protein folding.

24
Q

When proteins are broken down to amino acids in your stomach and small intestine, we would say that the protein has been:

A

Hydrolyzed

25
Cell membrane integral proteins typically have:
Alpha-helices with hydrophobic -R groups
26
Cilia and flagella are
A. Function in cellular motility B. Have a distinct 9+2 arrangement of microtubules C. Are basically the same thing, only that flagella are fewer in number and longer
27
Which of the following membranes is the most fluid?
A membrane composed of unsaturated fats only | Cholesterol makes cells slightly rigid
28
Which of the following structures of a plant cell are involved in the maintenance of turgor pressure?
A. Cell Wall B. Central vacuole
29
Which of the organelles is most involved packaging and distribution of proteins?
D. Golgi apparatus
30
Increasing the amount of substrate present will increase the rate of a reaction. True or False?
This is true until a plateau is reached and the enzyme can't move any faster. All excess enzyme can play a role in allosteric inhibition.
31
Is it true that only one enzyme substrate can every fit an active site?
No, there can also be competitive inhibitors.
32
What does cholesterol do?
Without cholesterol, cell membranes would be too fluid, not firm enough, and too permeable to some molecules. In other words, it keeps the membrane from turning to mush.
33
Do prokaryotes engage in cellular respiration?
Yes
34
Does the cell wall prevent expansion?
No, but it might prevent a cell form bursting.
35
How does pH interfere with a protein's secondary and tertiary structure?
It wrecks the hydrogen bonds
36
What is the only way to change the primary structure of proteins?
to break bonds
37
What is a lipid micelles?
When phospholipids form themselves into a circle
38
How to fats form?
Via a condensation reaction. Also called a dehydration reaction.
39
Do archea have membrane bound organelles?
NO!
40
Do archaea have eukaryote like gene structure and ribosomes?
Yes!
41
Compare and contrast archaea and eukaryotes?
They both have similar type ribosomes and gene like structures, but archaea lack membrane bound organelles
42
Do bacteria have a cell wall?
Yes
43
What is the relationship of the nuclear envelop to the er?
They are continuous
44
What do microfilament resist?
pull
45
What di microtubules resist?
push
46
What cytoskeletal component provides tracks for intercellular transport?
microtubules
47
What moves cilia and flagella?
microtubules
48
What cytoskeletal structure does the following: 1. ) provide structural reinforcement 2. ) anchor organelles 3. ) Kepp nucleus in place
Intermediate fibers
49
What motor protein moves along microtubules?
kinesin
50
Describes microtubules?
Hollow tubes. They are important in resisting compression They provides tracks for motor proteins They both anchor and allow for movement of organelles
51
What are cilia and flagella made of?
microtubules
52
Describe the shape of cilia?
short, numerous, complex
53
Describe the shape of flagella?
longer, fewer and less complex
54
Where is the site of aerobic respiration?
the mitochondria