Module 1 Flashcards

1
Q

What are the properties of living organisms

A

Order

Energy Processing

Sensitivity or response to stimuli

Reproduction

Growth and Development

Regulation/Homeostasis

Adaptation

Evolution

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2
Q

What is order?

A

Life is cell based, with a complex organisation which all works together to form life

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3
Q

What is energy processing

A

Capture energy from sun or other sources and convert it into chemical energy in food or use chemical energy from food

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4
Q

What is sensitivity or response to stimuli

A

Responding to stimuli such as touch or sun (for plants)

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5
Q

What is reproduction

A

Transferring DNA (from parental to daughter cells)

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6
Q

What is regulation/homeostasis

A

The set of internal conditions maintained by living things despite a changing environment

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7
Q

What is adaptation

A

Allows organisms to survive better in their environment by changing their behaviours are features to adapt to environment

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8
Q

What is the main difference between a eukaryote and a prokaryote

A

Eukaryotes have a defined nucleus where the DNA is kept, whereas prokaryotes don’t have a defined nucleus

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9
Q

What is an important element for life?

A

Carbon.

Life is carbon based. Carbon can bond with itself and other elements in different ways

All major biopolymers have a carbon backbone

However, there are some other useful elements such as Hydrogen, Nitrogen, Oxygen, Phosphorous and Sulfur which are important to life

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10
Q

Describe the hydrophobicity and polarity of C

A

C is neutral and non-polar/hydrophobic

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11
Q

Describe the hydrophobicity/polarity of O, N, P and sometimes S

A

They make compounds polar/hydrophillic, partly (dipoles) or fully charged

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12
Q

What does polar mean

A

It is a molecule with a charge on one side of the molecule

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13
Q

What does hydrophillic mean

A

It means that a molecule ‘loves water’, and have a tendency to mix and dissolve in water

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14
Q

What does non-polar mean?

A

there are no positive or negative poles formed in the molecule. The charges are equally distributed across a molecule

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15
Q

What does hydrophobic mean?

A

It means that a molecule ‘hates water’, and thus doesn’t have a tendency to mix

I.e. oil

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16
Q

What are the main building blocks of life

A

Water, carbohydrates (sugars), lipids, amino acids and nucleic acids

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17
Q

Explain the importance of water as a building block of life

A

We are ~62% water. It is a good solvent of polar molecules

Water helps stabilise body temp (good evaporative cooling, buffers temp change as freezing water releases energy and melting water absorbs it)

Ice floats (layers of ice can insulate water underneath / floating platforms)

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18
Q

Explain the composition of carbohydrates/sugars

A

Composed of C, H, O with the general formula C(n) (H2O) (n), where n is the no. of carbon atoms

Lots of ‘O’ means a very polar molecule

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19
Q

What is the function of carbohydrates/sugars?

A

Sugar polymers play an important role in life.

Starch - storage
Chitin - protection
Cellulose - structure
Bacterial cell walls/surrounding coats

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20
Q

What are lipids, and what do they do

A

Lipids are fatty compounds that perform a variety of functions in your body. They consist of a vast set of molecules, such as fats, oils, waxes, steroids. However, they are poorly soluble in water, whereas they are normally soluble in organic solvents

They’re part of your cell membranes and help control what goes in and out of your cells. They help with moving and storing energy, absorbing vitamins and making hormones.

They can act as energy stores, signal molecules, protect and act as waterproofing, and also function as structures/barriers (i.e. phospholipids barriers)

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21
Q

What are saturated lipids vs unsaturated lipids

A

saturated = all single bonds

unsaturated = one or more double bonds

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22
Q

Explain what a nucleic acid is and what it does

A

Nucleic acids are normally made up of nucleotides. These contain a phosphate group (negatively charged), and a nucleobase (A,C,T,G,U)

Their function is for genetic information storage (DNA), protein synthesis (RNA), and has regulatory functions.

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23
Q

What are biopolymers

A

polymers are made up of the same repeating units. Biopolymers are unique as they contain information unlike normal polymers.

Examples include DNA, RNA and proteins

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24
Q

What is the conventions of direction/ends of proteins

A

Proteins have an N terminus and C terminus. the N terminus is an amino acid group (and is basic). The C terminus is a carbonyl group (and is acidic)

The N terminus is the start of the protein, whereas the C terminus is the end of the protein

So gaps in protein are filled with anything as long as it goes from N terminus to C terminus

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25
Q

What is the conventions of direction/ends of nucleic acids

A

Here, they have a 5’ (5 prime), and a 3’ (3 prime) end.

Nucleic acid sequences are conventionally named from the 5’ end to the 3’ end

In this case, the 5’ is the start of the nucleic acid, and the 3’ is the end

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26
Q

What are the common features of nucleic acid polymers (DNA/RNA)/ what are the chemical components

A

Involves nucleotide building blocks (phosphate, sugar, base/nucleobases)

Common phosphate sugar backbone (sugars and phosphates are hydrophillic, and the phosphate is negatively charged)

5’ and 3’ ends

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27
Q

What are the common features of proteins/peptides?/ what are the chemical components?

A

Amino acid building blocks

Common peptide backbone (N-C-C)

Sidechains (R) of different amino acids are also different

Peptides if short have <50 amino acid residues, but long ones have >50 residues (but no strict definition

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28
Q

What is the difference between DNA and RNA

A

In RNA, the amino acid “thymine” doesn’t exist, instead there is only “uracil” (It becomes an A-U bond instead of an A-T bond in RNA compared to DNA)

Also, the chemical structure of RNA is that it has an OH at the bottom, whereas there is only an H at the bottom of DNA

DNA consists of two strands in a double helix, however, RNA only has one strand - both made up of nucleotides

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29
Q

Explain the properties of sugar phosphate backbone which is essential in nucleic acids

A

The backbone is composed of alternating sugar and phosphate groups, which form covalent phosphodiester bonds between the 3’ carbon of one sugar and the 5’ carbon of the next. This strong bond structure provides high stability, allowing nucleic acids to withstand various cellular conditions without breaking down easily.

The phosphate groups in the backbone carry a negative charge, which helps prevent the nucleic acids from folding into tight coils by repelling each other.

The backbone’s sugar and phosphate groups are hydrophilic (water-loving), making the exterior of the DNA double helix water-soluble. This property allows DNA to interact with the aqueous cellular environment and various proteins and enzymes.

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30
Q

Describe the repeating units in proteins

A

Proteins are made up of repeating units called amino acids, which connect in a linear chain to form a polypeptide. Each amino acid consists of two main parts: the backbone and the side chain (or R group). Together, these components give proteins their unique properties and functions.

The backbone of the protein has an amino group on the N terminus, which bonds to an alpha carbon (central carbon atom), which serves as a place for bonding to a side chain (R group). This also bonds to a carboxyl group (-COOH) at the end of the protein

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31
Q

How do peptide bonds forms?

A

Two amino acids react by condensation to form a dipeptide. This is energetically unfavourable, so it doesn’t happen spontaneously

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32
Q

Describe the sidechains in proteins (amino acids)

A

They have varied properties such as:

Size/shape, hydrophobicity, change, aromaticity, polarity, redox sensitivity, hydrogen bonding potential, flexibility

A small peptide combines various amino acid subgroups and thus combines many different properties such as the ones above. These all have different effects

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33
Q

Describe how the physical and chemical properties of proteins and nucleic acids can be exploited in
experimental situations

A

We can monitor the purity of DNA samples by checking ratios of absorbance values for likely contaminating molecules through A260 and A280

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34
Q

What can a A260:A280 ratio tell us

A

1.8-20 = pure dna

<1.8 = protein contamination

> 1.8 = RNA contamination

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35
Q

What can a A260:A230 ratio tell us?

A

> 1.8 = pure nucleic acid

<1.8 = Organic compounds

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36
Q

Is DNA a source of genetic information

A

Yes

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37
Q

What are the nucleobases used in DNA and RNA

A

DNA: Adenine (A), cytosine (C), guanine (G), Thymine (T)

RNA: Adenine (A), cytosine (C), guanine (G), Uracil (U)

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38
Q

What are the base pairings

A

A with T (DNA)

A with U (RNA)

C with G (DNA and RNA)

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39
Q

Is the number of A equal to something?

A

number of A is equal to number of T

Number of c is equal to number of G

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40
Q

Is A-T or C-G stronger?

A

C and G have 3 hydrogen bonds between them –> stronger binding

Compared to A and T/U which have 2 hydrogen bonds between them –> weaker binding

Thus, the G/C base pairing is stronger than the A/T(U) base pairing in nucleic acids

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41
Q

Describe the double helical structure of DNA

A

Strands run in opposite directions. Negative phosphates repel each other –> DNA spreads out

Major and minor grooves are present

Right handed double helix (twists clockwise when viewed from the top)

DNA has a right-handed double-helix shape, with two strands twisted around each other. The structure consists of a sugar-phosphate backbone on the outside and complementary base pairs (A-T and G-C) on the inside, held together by hydrogen bonds. The twisting creates major and minor grooves, which allow proteins to interact with the DNA for processes like gene regulation. This stable yet flexible structure is crucial for DNA’s role in storing genetic information.

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42
Q

What is the difference between major and minor grooves

A

Major Groove: This groove is wider and deeper, occurring where the backbones of the two DNA strands are further apart. It exposes a larger portion of the nitrogenous bases.

Minor Groove: This groove is narrower and shallower, occurring where the backbones are closer together. It exposes less of the nitrogenous bases.

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43
Q

Distinguish DNA from RNA in terms of structure and stability

A

DNA has a H at the bottom, whilst RNA has an OH at the bottom. DNA lacks an O which is present in RNA

DNA is also double stranded, whilst RNA is single stranded

DNA has A,C,T,G whilst RNA has A,C,U,G

RNA is less stable than DNA (because it has an OH group, which makes for more chemistry happening at OH, making it more susceptible to degradation/breakdown )

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44
Q

What is the central dogma of molecular biology

A

The central dogma of molecular biology is a theory stating that genetic information flows only in one direction, from DNA, to RNA, to protein, or RNA directly to protein.

We can’t go direct from DNA to protein - it has to go through RNA

We also can’t go back from protein to RNA

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45
Q

What are the key components of the central dogma?

A

The genome (the DNA)

The transcriptome (the RNA)

The proteome (the protein)

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46
Q

How does information flow between DNA, RNA and proteins?

A

The DNA undergoes transcription into RNA, and that in turn undergoes translation to form proteins (which are amino acids)

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47
Q

What is the genome

A

The genome is the complete set of genetic material in an organism, encompassing all of its DNA, including coding regions (genes) and non-coding sequences.

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48
Q

What is the transcriptome

A

The transcriptome refers to the complete set of RNA transcripts produced from the genome at a specific time or under specific conditions.

It includes all types of RNA, such as messenger RNA (mRNA), ribosomal RNA (rRNA), transfer RNA (tRNA), and non-coding RNAs (like microRNAs).

The transcriptome reflects gene expression, indicating which genes are actively transcribed into RNA in a given cell type, tissue, or developmental stage, thereby providing insight into the functional state of the cell.

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49
Q

What is the proteome

A

The proteome is the entire set of proteins that are expressed and modified in a particular cell, tissue, or organism at a given time.

It encompasses not only the proteins encoded by the genes in the genome but also variations due to post-translational modifications (e.g., phosphorylation, glycosylation) that affect protein function and activity.

Ultimately, it is all proteins expressed from the transcriptome, including their modifications

For example, they include ion channels, receptors, antibodies, enzymes etc

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50
Q

What is the difference in size and construction between bacterial and eukaryotic genomes?

A

Most bacteria (and prokaryotes) have circular chromosomes. They also tend to be relatively small. They are singular, circular chromosomes

However, eukaryotes have big genomes (multiple, linear chromosomes, condensed into chromatin and wrapped around histone proteins)

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51
Q

Describe features of the human genome

A

Eukaryotic and linear

Encodes ~20 000 proteins

6 billion base pairs

22 pairs of chromosomes (plus sex chromosomes)

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52
Q

What does mRNA do?

A

It is the messenger for making proteins.

It often makes multiple copies, and is designed to be used then degraded. It allows for cytosine deanimation to uracil

Degradation via the ribose

OK to be less stable than DNA. mRNA production rates vary

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53
Q

What are proteins

A

They are determined by a specific amino acid sequences which determines structure, and also the function

Proteins make up 50% of cell by dry weight, and give the cell its shape by forming receptors, enzymes, hormones, growth factors etc.

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54
Q

What is the universal genetic code

A

The universal genetic code is the set of rules by which genetic information encoded in DNA (or RNA) is translated into proteins. It defines how sequences of three nucleotide bases, called codons, correspond to specific amino acids or signal the termination of protein synthesis.

Ultimately, the universal genetic code features triplets (of bases) to form a codon. It is also non-overlapping (meaning that we read genetic code in triplets - three nucleobases at once)

Some amino acids can also have more than one code (there is some redundancy in the code)

The genetic code is degenerate or redundant, and is universal (used by all life forms)

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55
Q

What is the required codon for a protein to ‘start’

A

You need AUG codon, which goes on to form a MET amino acid. There is only one codon which can ‘start’ the formation of the protein

However, AUG can encode Met even in the middle of a protein sequence

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56
Q

What is a reading frame

A

A reading frame in a nucleic acid sequence refers to the way nucleotides are grouped into consecutive, non-overlapping triplets (codons) for translation into a protein. Each reading frame starts from a specific nucleotide and determines how the sequence is read and interpreted during protein synthesis.

In summary, a reading frame is a specific grouping of nucleotides into codons that dictates the amino acid sequence during translation. Selecting the correct reading frame is essential for accurate protein synthesis.

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57
Q

How do you select the right reading frame?

A

You want to try and identify the start codon (which is typically AUG), and then after that, the codon reads in triplets, so you want to keep following the triplet codons until you find a stop codon. This is normally how you identify the correct reading frame

The initial amino acids of the reading frame might not necessarily have to be a set of 3, because it all depends on what enables AUG to be found (have to look at booklet to understand)

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58
Q

What is the open reading frame

A

It is the region from the start to the stop codon of a gene. However, the STOP codon doesn’t encode an amino acid

59
Q

What are the different types of mutations

A

Point
Silent
Nonsense
Insertion
Deletion
Missense
Frameshift
Duplication

60
Q

What is a point mutation

A

Mistake in the DNA code, one of the DNA base pairs is changed

61
Q

What is a silent mutation

A

A mutation of the protein coding region that has no effect on the protein sequence

62
Q

What is a nonsense mutation

A

Single change in DNA code produces a stop codon, prematurely terminating protein synthesis

63
Q

What is an insertion mutation

A

Addition of one or more nucleotide base pairs into the DNA sequence

64
Q

What is a deletion mutation

A

A piece of DNA is removed from the sequence

65
Q

What is a missense mutation

A

A single amino acid has been changed

66
Q

What is a frameshift mutation

A

Insertion or deletion mutation results in change to a gene’s reading frame

67
Q

What is a duplication mutation

A

Incorrect copying leads to repeated sequences

68
Q

What is the general mechanism for copying DNA to DNA before cell division - replication?

A

1) Initiation (where/when/how to start)

2) Chain elongation (forming long polymers)

3) Termination (where/when to stop)

Note: there is an “origin” of replication for initiation (i.e. the spot where we start copying DNA)

Also, note that it involves a template for base pairing, and the newly synthesised strand is complementary to template strand.

The whole process uses a DNA polymerase (enzyme). We need a primer (short piece of DNA/RNA to start)

69
Q

What is a DNA polymerase - what is its function

A

Makes a DNA copy from a DNA template. Needs a primer to start.

proof reads the last nucleotide added –> has exonuclease activity to remove mismatched nucleotide –> decreased rates of something wrong happening

70
Q

How can helical DNA be unwound?

A

Pulling long heical strands apart causes supercoiling. To address this, the topoisomerase enzymes cut strands, allowing it to unwind and stick back together, and ultimately reduce supercoiling. In cells topiosmerase only unwinds small sections of DNA at a time

71
Q

What are some problems associated with replication?

A

DNA is a double-helix with strands tightly wound around each other, making it challenging to separate for replication.

As helicase unwinds the DNA, it causes supercoiling and tension further along the DNA molecule, which could impede replication.

DNA polymerase, the enzyme that synthesizes new DNA strands, can only add nucleotides to an existing strand and requires a 3’-OH group to initiate synthesis.

DNA strands are anti-parallel, meaning one strand runs 5’ to 3’ (leading strand), while the other runs 3’ to 5’ (lagging strand). DNA polymerase can only synthesize in the 5’ to 3’ direction, creating challenges for the lagging strand.

Mistakes in replication could lead to mutations, affecting the integrity of the genetic information.

72
Q

What was the strategy used to overcome the problem of ‘ DNA is a double-helix with strands tightly wound around each other, making it challenging to separate for replication.’

A

Helicase Enzyme: Helicase unwinds the DNA at the replication fork by breaking the hydrogen bonds between the two strands, creating two single-stranded templates for replication.

73
Q

What was the strategy used to overcome the problem of ‘ As helicase unwinds the DNA, it causes supercoiling and tension further along the DNA molecule, which could impede replication.
.’

A

The use of topoisomerase: Topoisomerases relieve the supercoiling tension by temporarily breaking one or both DNA strands, allowing the DNA to relax, and then rejoining the broken ends. In this way, topoisomerases prevent DNA tangling and damage during replication.

74
Q

What was the strategy used to overcome the problem of ‘ DNA polymerase, the enzyme that synthesizes new DNA strands, can only add nucleotides to an existing strand and requires a 3’-OH group to initiate synthesis.’

A

Primase Enzyme: Primase synthesizes a short RNA primer with a free 3’-OH group to serve as a starting point for DNA polymerase. This primer is later replaced with DNA.

75
Q

What was the strategy used to overcome the problem of ‘DNA strands are anti-parallel, meaning one strand runs 5’ to 3’ (leading strand), while the other runs 3’ to 5’ (lagging strand). DNA polymerase can only synthesize in the 5’ to 3’ direction, creating challenges for the lagging strand.’

A

Leading Strand Synthesis: The leading strand is synthesized continuously in the same direction as the replication fork.

Lagging Strand Synthesis: The lagging strand is synthesized discontinuously in short fragments known as Okazaki fragments. Each fragment requires its own RNA primer. DNA polymerase synthesizes these fragments in the 5’ to 3’ direction, moving away from the replication fork.

Joining Okazaki Fragments: Once the fragments are synthesized, DNA polymerase I removes the RNA primers and replaces them with DNA. DNA ligase then joins the fragments together by forming phosphodiester bonds, creating a continuous strand.

76
Q

What was the strategy used to overcome the problem of ‘ Mistakes in replication could lead to mutations, affecting the integrity of the genetic information.’

A

Proofreading by DNA Polymerase: DNA polymerases have a proofreading ability. They can detect mismatched nucleotides and remove them using their 3’ to 5’ exonuclease activity before continuing DNA synthesis, which enhances the fidelity of replication.

77
Q

Describe the functions of DNA helicase

A

Helps unwind the DNA double helix

78
Q

Describe the functions of DNA topisomerase/gyrase

A

Helps reduce supercoiling by temporarily breaking one or both DNA strands, allowing the DNA to relax, and then rejoining the broken ends. In this way, topoisomerases prevent DNA tangling and damage during replication.

79
Q

Describe the function of Single stranded binding proteins

A

Coat single stranded DNA to keep strands apart / stop small segments of basic pairing / protect DNA

80
Q

Describe the function of DNA polymerase

A

Lay down the DNA which is complementary to the template

DNA polymerase III = the main one laying down the DNA

DNA polymerase I = the one which removes RNA primers and replace it with DNA

81
Q

How many replication forks are there ?

A

2

82
Q

How many strands are copied at a replication fork

A

A lagging and leading strand (2 strands)

Thus, it would have 4 total replications occurring

83
Q

Explain the process of Leading Strand replication

A

The gyrase/topoisomerase goes ahead on the dna and releases supercoiling, followed by the helicase which pulls the DNA strand apart. A primaseis placed at the start of the leading strand, which places down an RNA primer.

DNA polymerase 3 then synthesises DNA from that RNA primer, and continues extending. As helicase unwinds the strand continues to be copied.

This is all occurring simultaneosuly to lagging strand replication

Here, the replication is going towards the replication fork

84
Q

Explain the process of the lagging strand replication

A

A primase also places down a complementary RNA primer to the lagging strand. However, instead of DNA synthesis going towards the helicase, here the DNA synthesis is going away from the replicaiton fork (because it has to be a 5’ to 3’ dna synthesis)

The primase also places other RNA primers as the helicase unwinds the DNA. This leadas to a couple RNA primers next to the lagging strand. The DNA polymerase III makes lots of small fragments of DNA between the RNA primers. These are called OKAZAKI FRAGMENTS because they aren’t joined to primases yet

DNA polymerase I comes and removes the RNA primers and fills them in with DNA

DNA ligase joins the DNA fragments to make the lagging strand complete

85
Q

How are the ends joined in circular chromosomal DNA

A

1) DNA polymerase 3 reaches the RNA primer

2) DNA polymerase 1 removes RNA primer and replaces it with DNA

3) DNA ligase joins the ends of the DNA

4) completed strand

86
Q

What is the very basic mechanism of transcription (DNA to RNA)

A

RNA polymerase makes an RNA copy from a DNA template. Doesn’t need a primer to start

87
Q

What are features of RNA polymerase

A

Doesn’t need a primer to start

Limited proofreading - increased chances of error

88
Q

What are the unique problems associated with transcription?

A

Where to start? (initiation)

How are they made? (elongation)

Where to stop? (termination

How to switch on/off/upregulate?

89
Q

How does initiation process work

A

Transcription begins at specific DNA sequences called promoters, located upstream of the gene. In eukaryotes, the promoter often includes a TATA box.

This TATA bbox is easy to melt, and it is the promoter region where RNA polymerase must bind to transcribe the gene

RNA polymerase associates with DNA bound transcription factor (s) which are proteins capable of recognising a specific base sequence - in this case it is the TATA box. They are able to help facilitate the binding of RNA polymerase to the single stranded DNA. The DNA is “melted” in the local region

90
Q

How does the elongation process work

A

Using the DNA template strand, RNA polymerase adds complementary RNA nucleotides (adenine, uracil, cytosine, and guanine) in the 5’ to 3’ direction, building an RNA strand.

RNA polymerase moves along the DNA, continuously synthesizing RNA as it unwinds and rewinds sections of the DNA, allowing only a small region to remain open at a time. This small region is called the transcription bubble (in here, the two strands of DNA are separated - one is a template strand and the other isn’t )

This ultimately continues

91
Q

How does the termination process work?

A

Transcription stops when RNA polymerase encounters a specific termination sequence in the DNA.

For example a G/C rich region , followed by an A/T rich sequences can form a ds hairpin structure, causing transcription to pause and the RNA polymerase to dissociate and the RNA be released

OR

a Rho protein binds, and uses helicase activity to travel up to and dissociate the DNA/RNA hybrid complex (physically pull or force apart the protein nucleic acid complex) - the RNA dissociates from DNA template

92
Q

How can transcription be regulated?

A

Repression
Accelerator

93
Q

How can transcription be repressed?

A

A protein repressor binds. This blocks the binding of the sigma factor / transcription factor –> no RNA polymerase binding –> no transcription and thus no gene expression

94
Q

How can transcription be accelerated?

A

Sigma factor / transcription factor doesn’t bind strongly/often. However, a transcriptional activator (a protein) can bind at a specific DNA sequence and alter the structure of the promoter so that transcription factor can now bind more frequently –> accelerates transcription

95
Q

How are repressors and activators modulated?

A

Often modulated by small molecule binding (often metabolites)

96
Q

What are the unique problems associated with converting information as a nucleic acid sequence to an amino acid sequence

A

Need to somehow convert a sequence of nucleotides (A,C,T,G,U) to a sequence of amino acids –> need to adopt a different chemistry - we can’t rely on base pairing to do this.

We also need to have a correct order of amino acids

Peptide bonds formation is very thermodynamically unfavourable

97
Q

What are the 3 types of RNA

A

Messenger RNA (mRNA)

Transfer RNA (tRNA)

Ribosomal RNA (rRNA)

98
Q

What are aa-tRNA synthases?

A

WOrk with tRNA, and they essentially make sure the right amino acids is attached to the tRNA

These recognise amino acid, anticodon and other parts of tRNA. Attaches correct amino acid to its matched tRNA

They also give ijt the energy to overcome the unfavourable thermodynamics associated with forming a peptide bond

Ultimately the synthetases allows the tRNA to transform into an aa-trna to be used

99
Q

What does the mRNA do

A

Contains template for protein synthesis / information about which amino acids to be added in which order (i.e. the RNA strand which was produced)

100
Q

What does the tRNA do

A

Matches the correct amino acid to the template

There are different tRNAs for each amino acid/ codon combination

Decodes mRNA sequence to protein

101
Q

What does the rRNA do

A

Combines with proteins to form the machinery for protein synthesis / catalyses peptide bond formation

102
Q

What is a ribosome and how does it work

A

It consits of small and large subunits, and enzymes

The A-site accepts income tRNA, and the amino acid is deposited in the P-site, before the remainder of the tRNA is moved to the E-site to exit

103
Q

What are the 3 stages of protein synthesis in the ribosome

A

Initiation

Elongation

Termination

104
Q

Explain the process of Initiation

A

Small subunit of ribosome binds mRNA and Met-tRNA. This initiates everything, and the large subunit of ribosome binds

105
Q

Explain the process of elongatin

A

The tRNA comes in guided by anticodon/codon matching. Activated amino acids are positioned next to each other. Since they are ‘activated’, they can use the energy stored in the aa-trna bond.

Peptidyl transferase in ribosome catalyses peptide bond formation using energy stored in the aa-trna bond. Te first tRNA is then released, and the ribosome moves along to the next codon on mRNA etc

106
Q

Explain the process of termination

A

When stop codon is reached, no tRNA matches - a release factor (protein) binds. Fromm here, peptidyl transferase from ribosome adds water instead of an amino acid –> releases the polypeptide

107
Q

What are two problems associated with protein synthesis

A

Unfavourable thermodynamics of peptide bond formation

Requirement for order

108
Q

How is the problem with unfavourable thermodynamics addressed

A

Cells use a class of enzymes called aminoacyl-tRNA synthetases to couple each amino acid to its corresponding transfer RNA (tRNA) molecule, a process that requires ATP.

Energetically Favorable: This reaction creates an aminoacyl-tRNA complex, an “activated” form of the amino acid that can readily participate in peptide bond formation on the ribosome.

109
Q

How is the requirement for order addressed

A

tRNA and mRNA Matching: Each amino acid is added to the growing polypeptide chain according to the mRNA sequence. The ribosome reads mRNA codons, and the corresponding aminoacyl-tRNA with the matching anticodon is selected.

110
Q

What is a primary protein structure

A

It consists of the amino acid sequence of a protein - the very basic form of an amino acid

111
Q

What is a secondary protein

A

Describes the local structures (e.g. Alpha helix, and beta sheet)

It has backbone-backbone hydrogen bonding interactions which are important for it structure

Sidechains also help hold structure together

112
Q

What is a tertiary protein structure

A

Overall 3D arrangement of a polypeptide chain (i.e. combining secondary structures)

Held together by a lot of different interactions / bonds such as hydrogen bonds, iconic/electrostatic and polar interactions

Hydrophobic interaactions here, and it is a driving force for protein folding (force which groups nonpolar segments of molecules and polar sements of molecules together)

ph, solvents and temp are really important for maintaining structure here

113
Q

What is a quarternary protein

A

Organisation of subunits (many but not all proteins have multiple subunits) (i.e. multiple polypeptide chains)

114
Q

WHat are alpha helices?

A

They are the basic right handed helixes. They have their sidechains pointing outwards of the helix

115
Q

What are beta sheets

A

These are expressed as arrows which points in direction of protein chains (i.e. from N to C )

They have their sidechains pointing above and below, ultimately creating a tangle of sidechains within the beta sheet. (compared to alpha helix, this is more chaotic in terms of sidechains)

116
Q

Protein folding

A

information encoded in amino acid sequence

Burial of hydrophobic surfaces/sidechains in aqueous solvent

collapse of protein chain / formation of secondary structure

Firming up tertiary structre by interactions between different parts of protein

Not much extra space in protein after folding

Protein folding is crucial because it determines a protein’s three-dimensional shape, which directly impacts its function. Proteins must fold into specific shapes to perform their roles correctly within a cell, as their structure enables interactions with other molecules

117
Q

Appreciate that the protein sequence defines the protein fold and function, and that
protein molecules are held together by the combination of many bonds

A
118
Q

Demonstrate how 3D protein structure is related to function using the example of the
alpha helix in DNA binding proteins.

A
119
Q

What is energy

A

Capacity to do work

120
Q

What is potential energy

A

Potential energy is a form of stored energy which has the potential to be turned into other types of energy like kinetic energy

121
Q

What is kinetic energy

A

Kinetic energy is the energy an object possesses due to its motion. Any object that is moving, regardless of direction, has kinetic energy because of its velocity and mass.

122
Q

What is entropy

A

Measure of disorder in a system

123
Q

What is classified as a favourable reaction

A

A favourable reaction will typically be exergonic - releasing energy

124
Q

What is classified as an unfavourable reaction

A

An unfavourable reaction will typically require energy input (endergonic) - absorbing energy

125
Q

What is equilibrium

A

It is when the rate of the forward reaction is equal to the rate of the reverse reaction, without the concentrations of the products and reactants necessarily having to be the same

All chemical equations attempt to reach equilibrium

126
Q

How does equilibrium link to cells

A

In living cells, reactions will never reach equilibrium. This is because new substrates are added, and products are used up which all ruin equilibrium

127
Q

How does equilibrium relate to energy

A

Equilibrium shifts to favour the reaction which utilises the least energy (?!)

128
Q

what is thermodynamics

A

Thermodynamics is the study of energy changes and the direction in which energy flows in a system. It deals with the relationship between heat, work, temperature, and energy in a system, and it helps predict whether a process or reaction is energetically favorable.

Law of thermodynamics

129
Q

what is kinetics

A

Kinetics is the study of the rate at which a reaction occurs and the factors that affect that rate. It focuses on how quickly or slowly a reaction proceeds and the mechanisms involved in the process, such as the steps through which reactants are converted into products.

I.e. Activation energy, catalysts, reaction rates

130
Q

Explain the difference between thermodynamic and kinetic properties of a reaction

A

Kinetics focus on pathway from reactants to products. Ultimately decides how fast a reaction will take. (Activation barriers)

Meanwhile, thermodynamics deals with eenergetics and equilibrium of reactions, ultimately indicating direction and final state of reaction

Thermodynamic properties focus on the overall energy change and stability of the reactants and products., Kinetic properties describe the rate of the reaction and the mechanism (pathway) by which it occurs.

131
Q

How can enzymes act as a catalyst

A

Assist in lowering the energy barrier - they are biological catalysts. This results in the reaction rattes being sped up

132
Q

Explain the effect of enzymes on the concentrations of substrates and products of a reaction

A

Enzymes have no effect on the end concentrations, however it just allows the reaction to proceed faster

133
Q

What are 3 ways to explain enzyme binding

A

Lock and key model

Induced fit model

Selection model

134
Q

What is the lock and key model

A

Substrate molecule fits directly into the active site

135
Q

What is the induced fit model

A

Substrate induces a shape change for optimal substrate binding and activity

136
Q

What is the selection model

A

The selection model for enzyme function, sometimes referred to as conformational selection, proposes that enzymes exist in multiple conformations (shapes) even before they bind to a substrate. In this model, the enzyme “selects” the appropriate conformation that best fits the substrate when the substrate is present, rather than needing to change shape after binding.

137
Q

How are enzymes named

A

Typically have an “ase” ending

Naming system is based on their activity and what they assist in doing

138
Q

What are characteristics of enzymes

A

Biological catalysts

Mostly proteins (some RNAs are enzymes)

Highly varied in terms of function, size and ability to be regulated

Arent used up in a reaction

Highly specific for a substrate

Can be regulated

Mutations in enzyme can and will cause disease

139
Q

How are enzymes regulated

A

They have evolved to work best at specific temps and PH

Many require an additional chemical component (cofactor) for optimal activity

It could be inhibited by a compound that binds to the active site and prevents substrate binding OR binds outside the active site and stops the motion of enzymes required for activities

140
Q

Explain enzymatic pathways

A

ENzymes can accelerate pathways for metabolism, synthesis of cellular materials, communication (signals) etc

Mutations that decrease activity / change specificity / increase activity or alter regulation can cause disease

These are all necessary enzymatic pathways for living organisms

141
Q

Describe enzyme location

A

Partly regulated by compartmentalisation - can be found inside or outside cells, in particular cellular compartments

Enzymes in the wrong place can be a sign of a problem or cause a problem

142
Q

Describe how a secondary reaction can drive equilibrium and provide energy for an unfavourable interaction

A

A secondary reaction can drive equilibrium and provide energy for an unfavorable reaction by coupling it with a favorable reaction. This coupling allows the combined reactions to proceed by effectively “paying” the energy cost of the unfavorable reaction with the energy released by the favorable one. This principle is commonly seen in biochemical reactions and is essential for cellular processes that would otherwise be energetically impossible.

143
Q
A