DNA, RNA, Proteins Flashcards

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1
Q

illustrate transcription

A

initiation - TATA box binding protein bind to DNA, TFII + RNA polymerase II bind, transcription factors at enhancers trigger elongation

elongation - 5’ to 3’ with template strand, free nucleotides line up by comp base pairing -> pre-mRNA

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2
Q

illustrate splicing

A

in nucleus
capping at 5’ end for stabilisation , add polyA to 3’

splicing - removal of introns by spliceosome

alternative splicing - combination of diff exons give diff mature RNAs + proteins;one gene -> diff proteins

mature mRNA produced

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3
Q

illustrate translation

A

mature mRNA transported to ribosomes in cytoplasm

tRNA carries amino acid to ribosome, bind from A -> p -> E

rRNA catalyse formation of peptide bond between amino acid

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4
Q

what is the central dogma

A

DNA —transcription—> RNA —translation—> protein
<—reverses trans—

DNA undergo replication

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5
Q

diseases related to transcription + translation

A

anaemia - variation in HBB sequence (7th protein) A to T -> fibre formed + cell shape distorted -> cannot carry oxygen (hetero adv: carriers have 10-fold decreased chance of malaria)

thalassaemia - reduced alpha/beta-globin, lack of haemoglobin production

cystic fibrosis - salty skin, deletion of 3bp at 508 -> loss of Phe

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6
Q

nucleotide and nucleic acid structure

A

nucleotide - monomers of nucleic acid

consists of phoshpate, pentose, purine ( 2 carbon nitrogen rings, A/G), pyramidines (1 carbon nitrogen ring, C/T)

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7
Q

difference between dna and rna structure and function

A

2’ carbon of pentose - DNA = H, RNA = OH
DNA - T, RNA - U

DNA - double helix, anti parallel, major + minor grooves, phosphate + pentose backbone , bases inside

RNA - varied structure (>=2 nucleotides link tgt)

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8
Q

illustrate packaging of DNA by histones into nucleosomes

A

histone - protein providing structural support for chromosomes, DNA wrap around for compact shape

nucleosome - 8 core histone protein, spool-like for DNA to wrap around

DNA < nucleosome < beads-on-a-string chromatin

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9
Q

regulation of gene expression + importance

A
  1. transcription factors = bind to activator proteins -> form protein complex that binds to gene promoter -> for RNA polymerase to attach
  2. splicing
  3. histone modification - which DNA exposed to polymerase to turn on or off the histones

important for detecting expression of gene. to diagnose cancer progression

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10
Q

examples of genomic science and digital health in precision medicine

A
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11
Q

function of CRISPR-Cas9

A

a CAS9 protein bounded with sgRNA - identify + cut specific sections of DNA

for deactivating gene by cutting DNA + error prone repair of cell -> mutations disable gene

also add new genes / change specific base

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12
Q

important roles of protein in biomedicine

A

enzymes
nucleic acid interactions
receptors
provide structure to cells and tissues
antibodies in immune system

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13
Q

insulin + receptor interaction

A

insulin bind to outside part of receptor -> protein parts inside cell unwind + make contact for activation -> more glucose transporters inserted into cell membrane for increased glucose uptake

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14
Q

enantiomeric nature of amino acids

A

proteins made up of L-a amino acids

a - chiral molecule, diff mirror image
L - with H towards me, CORN in clockwise (D- CORN anticlockwise)

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15
Q

difference between 4 levels of protein structure

A

primary - amino acid sequence, read from nitrogen to carbon terminal

secondary - conformation of backbone, alpha helix + beta sheet

tertiary - 3D structure due to h-bond, vdw, electrostatic attractions

quaternary - >1 polypeptide chain forming final functional structure (eg haemoglobin)

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16
Q

alpha helix vs beta sheet

A

alpha helix - right handed spiral shape, can be single stranded

beta sheet - pleated sheet-like, must have =<2 strands, parallel/anti-parallel

17
Q

globular vs fibrous protein

A

globular - circular, soluble in aq sol, functional

fibrous - long narrow extended, structural

18
Q

structure of collagen and keratin

A

collagen - 3 left-handed alpha helix forming right-handed superhelix -> strong fibre, recurring Gly-Pro-hydroxyproline

keratin - 2 alpha helix chains form coil, stabilised by disulphide bridge, more Cys = more stable

19
Q

haemoglobin and myoglobin in oxygen transportty -

A

haem - prosthetic group to carry O2 (with Fe at centre)

myoglobin - monomeric, 1 haem, carry single o2

haemoglobin - tetrameric, 4 haem, positive cooperativity - increase affinity for o2 when more o2 is blinded

20
Q

carbon monoxide poisoning

A

CO binds to haem -> lock haemoglobin in high affinity R state -> cannot release o2 to myoglobin in tissues

21
Q

protein misfolding + diseases

A

prion diseases - normal PrPc convert to abnormal PrPSc; PrPSc are sites of nucleation -> infectious + small amount cause all to change
alzheimer disease - amyloid-beta peptide self-associate into fibrils then into amyloid plaques
diabetes type 2, huntington disease etc