Molecules of Life Flashcards

1
Q

What are the 4 main types of macromolecules

A
  • carbohydrates
  • proteins
  • nucleic acids
  • fats
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2
Q

What is the hydrophobic effect

A

the tendency of non-polar molecules to self-associate in water rather than to dissolve

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3
Q

What are zwitterions

A

molecule that has both positive and negative regions of charge

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4
Q

How does the hydrophobic effect favour ligand binding

A

binding sites are often hydrophobic and can bind hydrophobic substrates/ligands

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5
Q

Amino acids and stereoisomers

A
  • all amino acids are chiral
  • they have 2 mirror images D and L
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6
Q

What are some biologically useful properties of amino acids

A
  • capacity to polymerise
  • acid-base properties
  • chemical functionality
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7
Q

Outline primary structure

A

It refers to the amino acid sequence in a polypeptide chain

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8
Q

Outline the secondary structure

A

It refers to the folding of the polypeptide due to H bonds between amine and carboxylic groups
- H bonds provide structural stability via alpha helix or beta sheets

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9
Q

Outline Alpha Helix features

A
  • coiled structure with R groups projecting outwards
  • H bonds are inside helix makes extra stable
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10
Q

Outline Beta Sheets features

A
  • strands of a beta-sheet may be parallel or anti-parallel
  • H bonds link the strands in a beta sheet
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11
Q

Outline the tertiary structure

A
  • the twisting and folding of the polypeptide to form a specific 3D shape caused by interactions of the R groups
  • the native fold
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12
Q

Outline the quaternary structure

A

two or more separate polypeptides bind together

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13
Q

What are homo-multimers

A

same polypeptide chains bind together in quaternary structure

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14
Q

What are hetero-multimers

A

different polypeptide chains bind together in quaternary structure

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15
Q

What are features of fibrous proteins

A
  • long and narrow chains
  • insoluble in water, hydrophobic part on outside
  • structural role
  • provides strength and stability
  • more resistant in pH and temp
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16
Q

What are features of globular proteins

A
  • spherical form
  • hydrophilic part is on outside
  • functional role
  • soluble in water
  • sensitive to changes in pH and temp
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17
Q

Define denaturation

A

the loss of tertiary structure

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18
Q

What is the consequence of protein misfolding

A

diseases (ex: sickle cell + Alzheimer)

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19
Q

What is the central dogma

A

the flow of genetic information from DNA to RNA to proteins

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20
Q

How was the helical shape of DNA discovered

A

X-ray diffraction by Rosalind Franklin and Ray Gosling

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21
Q

What are features of DNA

A
  • double helix
  • anti-parallel strands
  • complementary base pairings
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22
Q

What is the name of the bond between nucleotides

A

phosphodiester linkage

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23
Q

What are pyrimidine

A

two carbon rings

24
Q

Name examples of pyrimidine

A
  • cytosine
  • thymine
  • uracil
25
Q

What are purines

A

one carbon ring

26
Q

Name examples of purines

A
  • guanine
  • adenine
27
Q

What are features of RNA

A
  • single strand
  • uracil
  • ribose sugar
28
Q

What are the main types of RNA

A
  • mRNA
  • rRNA
  • microRNA
  • tRNA
29
Q

What is the function of mRNA

A

they code for proteins

30
Q

What is the function of tRNA

A

they carry amino acids

31
Q

What is the function of rRNA

A

they catalyse protein synthesis + form core of ribosome’s structure

32
Q

What is the function of microRNA

A

they regulate gene expression

33
Q

What is the dual capacity of RNA

A
  • act as catalyst
  • carries genetic information
34
Q

What are ribozymes

A

they catalyse chemical reactions via transesterification or phosphodiester bond hydrolysis

35
Q

DNA strands melt at different temp. depending on what

A

the percentage of G-C pairings (3 H-bonds)

36
Q

What is the purpose of PCR

A

amplify DNA

37
Q

Outline the process of PCR

A
  1. Denaturation: DNA samples is heated at 95
  2. Annealing: DNA primers are added to target sequence
  3. Elongation: Taq polymerase binds to primers and copies strand at 72
38
Q

What is the sense strand

A

the strand of DNA which has the same sequence as the mRNA except uracil is replaced by thymine

39
Q

What is the anti-sense strand

A

the strand opposite to the DNA

40
Q

What is the start signal for transcription

A

the promoter region and the TATA box

41
Q

What is the purpose of post-transcriptional modifications

A

helps prevent degradationof mRNA

42
Q

Why don’t prokaryotes experience post-transcriptional modifications

A

translation occurs immediately after transcription

43
Q

What are 3 post-transcriptional events

A
  • methylated cap added
  • poly-A tail added
  • introns removed
44
Q

What can defects in splicing cause

A

genetic diseases

45
Q

What is a retrovirus

A

a virus that forms RNA into DNA

46
Q

HIV is an example of what

A

retrovirus

47
Q

What are the 4 types of mutation

A
  • silent
  • missense
  • nonsense
  • frameshift
48
Q

What are polysomes

A

several ribosomess used to translate an mRNA at the same time

49
Q

What to antibiotics target

A
  • cell wall
  • DNA & RNA synthesis
  • protein synthesis
50
Q

What are prions

A

they reverse the flow of genetic information from proteins to the genome

51
Q

What is the relationship between transcription factors and Major DNA Groove

A

transcription factors bind to Major DNA groove (more accessible)

52
Q

What are operons

A

a cluster of genes that are transcribed together to give mRNA, therefore encode multiple proteins (bacteria)

53
Q

What is combinatorial control

A

it requires the coordinated interactions of multiple proteins for gene expression

54
Q

What is hormonal control of gene expression

A

steroid hormones act as transcription factors to regulate gene expression

55
Q

Name chemical modification to histone tails

A
  • acetylation
  • methylation
  • phosphorylation
56
Q

What is the consequence of acetylation on histone tails

A

It causes DNA to be less tightly wrapped around histone

57
Q
A