Week 3 (needs friday prelecture content) Flashcards

1
Q

What do different base sequences result in?

A

Difference genes and thus proteins.

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2
Q

If a 5’ end has a 5’ carbon at it’s end, what does a 3’ end have?

A

A 3’ carbon.
5’ end ends in a phosphate group and 3’ in a hydroxyl group.

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3
Q

How do DNA strands run?

A

Antiparallel.

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4
Q

How do we find the orientation?

A

Using the ends (5’ and 3’).

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5
Q

What does a RNA look like?

A

It has irrelgular twists from H-bonds within the RNA molecule.

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6
Q

What does the mRNA sequence determine?

A

The shape of the protein, which is necessary for function.
Sometimes an RNA can be what is transcribed and made.

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7
Q

What is the strand opposite of the template strand called?

A

The sense strand. It is basically the same sequence as the RNA.

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8
Q

What is the structure of DNA?

A

A sugar phosphate backbone with nitrogenous bases ATCG. Each strand has a 5’ end and a 3’ end. - these primes refer to polarity.

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9
Q

For polysaccharides, what is an example of a monomer, polymer, and the type of linkage?

A

Glucose - starch, glycogen, cellulose - glycosidic linkage.

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10
Q

For nucleic acids, what is an example of a monomer, polymer, and the type of linkage?

A

Nucleotides - DNA/RNA/Oligonucleotides (a short polymer ~ 10-50 nucleotides) - phosphodiester linkage.

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11
Q

What is the name of the linkage that joins nucleotides to the nucleic acid?

A

Phosphodiester linkage.

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12
Q

What does one monomer of DNA include?

A

1 sugar and 1 phosphate, includes RNA & DNA. Nitrogenous base (?).

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13
Q

What are the size differences between A, T, G, C, and U?

A

C, T, U are smaller chemical structures, while G and A are larger.

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14
Q

Why is the 5’ end called the 5’ end?

A

Because the carbon at the end/coming off the ring is connected to a phosphate group.
For 3’, it is connectedto a hydroxyl group.

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15
Q

Why is the direction of the DNA strands important?

A

Enzymes that make nucleic acids only work in one direction. (5’ to 3’)

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16
Q

You can have a purine base x a purine (big) base, and pyrimidine x pyrimidine (small)? Yes or no.

A

No. Only Purine x Pyrimidine.

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17
Q

What type of bond is between bases in DNA?

A

Hydrogen bond.

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18
Q

DNA is … handed?

A

Right handed.

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19
Q

Explain DNA replication.

A

The double stranded DNA is unwound, and each strand is used as a templatre to form daughter molecules depending on what is complimentary. (only works because of redundency). Polymerase enzyme can only add to the 3’ end.

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20
Q

What is the central dogma?

A

DNA is transcribed to RNA that is transported to the cytoplasm and then translated into given protein.

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21
Q

What type of structure does RNA have?

A

A 3D structure as the RNA folds in on itseld - it only has one backbone/

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22
Q

What is genetic material?

A

Molecules that carry on genetic info to offspring.

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23
Q

What is the Hershey-Chase experiment?

A

The Hershey-Chase experiment, conducted in 1952, definitively demonstrated that DNA, not protein, is the genetic material passed from viruses to bacteria, using bacteriophages (viruses that infect bacteria) and radioactive labeling techniques.
(refer to Week 3 lecture 1 prelecture content)

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24
Q

What percentage of genome has protein encoding sequence?

A

1-2% of the DNA.

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25
Name some types of proteins/uses.
Enzymes, defensive proteins, storage (eg. storing amino acids for embryos to use), transport proteins, etc.
26
What percentage of dry mass in most cells do proteins account for?
More than 50%.
27
What is the monomer of the macromolecule Protein (polypeptide)?
Amino acids that connect with a peptide bond.
28
What do Amino acids generally contain?
An amino group, carboxyl group, and an R-group (side chain).
29
What is the primary structure of a protein?
The original polypeptide sequence of amino acids.
30
What is the secondary structure of a protein?
α helix or β pleated sheet, both of which depend on the Amino acid sequence.
31
What is the tertiary structure of a protein?
Entire 3D shape of polypeptide. Can make up a part of a whole protein or be the whole protein.
32
What is the quartinary structure of a protein?
Several polypeptide chains together to make one functioning protein.
33
What will a tiny difference in the DNA code do?
It has the chance to effect the shape and thus the function.
34
How important is structure?
It is basically everything, whether it is physical structure, an enzyme, or an antibody.
35
What determines the shape of a protein?
The amino acid sequence.
36
What determines the function of a protein?
The structure.
37
Types of structural models?
Space-filling model, Ribbon model, Wire-frame model. *solid or simple shape can be used if details aren't needed.
38
Is the structure of a protein permanent?
No. Most of the chemical interactions holding the structure together are not strong. They are highly susceptible to pH, salt concentrations, and high temperatures.
39
What happens when a protein is given conditions heavily outside of its optimal?
The shape will unravel - denature.
40
What does it mean if a protein is denatured?
The protein is biologically inactive - its 3D shape is lost.
41
What happens if you undo external changes to a denatured protein?
The protein may be able to renature.
42
What is an enzyme?
A catalyst that assists a chemical reaction where it begins with a specific molecule(s) and ends with a product(s). It can be breaking things down or binding things together.
43
What is a metabolic pathway?
Several enzyme reactions, where each step is catalysed by a specific enzyme/
44
What is Gibb's Free Eneregy?
ΔG. The energy available to do 'work' in a cell.
45
What is based on ΔG?
Whether a process is spontaneous or non-spontaneous.
46
What is important about the speed of a spontaneous reaction?
They can be both fast and slow, but enzymes increase the reaction speed.
47
What type of reaction is a spontaneous reaction?
An exergonic reaction as energy is released and ΔG is negative.
48
What type of reaction is a non-spontaneous reaction?
An endergonic reaction as energy needs to be taken in (energy in product has more than reactant), ΔG is positive.
49
What can the released energy in an exergonic reaction be used for?
The energy can be repurposed and used in non-spontaneous reactions.
50
What do enzymes do in a reaction?
Enzumes come in as there is often a hump of energy required called the activation energy that enzymes can reduce.
51
What are 3 types of work in a cell? (that ATP is used for)
Chemical work: pushing endergonic reactions. Transport work: pumping substances against concentration gradients. Mechanical work: eg. muscle cell contractions.
52
How important is ATP?
Everything in the cell is making or using ATP.
53
Where is ATP known from?
RNA - it is composed of ribose, adenine, and 3 phosphate groups.
54
What is ATP known as?
Energy currency.
55
How much Gibb's free energy does ATP have?
Very high amounts.
56
What happens when a phosphate in ATP is hydrolised and removed?
It is very exergonic and thus releases a lot of energy, becoming ADP.
57
Where does the energy change in ATP -> ADP come from?
The chemical chjange of state to lower free energy, not the phosphate bonds.
58
How can ADP return to being ATP?
It can be phosphorylated based on energy released by other exergonic/catabolic reactions in the cell.
59
What is an Enzyme?
A subset of proteins that catalyses reactions. It is a catalyst that is a chemical eagent that speeds up a reaction without beign consumed.
60
How does Enzyme naming work?
Names end in 'ase'.
61
How important is the shape to Enzyme?
Enzymes need to perfectly match with its substrate shape, eg bringing 2 reactants close together, lowering the activation energy?
62
Do enzymes affect ΔG?
No, they only speed up the reaction.
63
What are the steps for an enzyme in a cell?
1. Substrate enters the active site. 2. Substrates are held in active site by weak interactions. 3. Active site lowers activation energy. 4. Substrates become products. 5. Products are released. 6. Active site is ready for new substances.
64
What is it called when a substrate binds to an enzyme?
It is called an enzyme-substrate complex.
65
How well do enzymes and substrates match?
They usually match 1-1 as the reaction catalysed is very specific.
66
What is important to maintian enzyme structure?
Optimal temperatures and pHs.
67
What are the two types of inhibitors?
Competitive (binds to the active site), non-competitive (binds elsewhere and changes the shape of the enzyme).