Biochemistry: From DNA to Protein Flashcards

1
Q

genome

A

all the DNA in each cell

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2
Q

nucleoside

A

base and sugar

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3
Q

nucleotide

A

nucleoside and phosphate

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4
Q

where do phosphodiester bonds occur

A

between the free 3’ OH and 5’ triphosphate of two nucleotides

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5
Q

how do nucelotide analogues work as drugs

A

have a higher affinity for viral DNA than human and stop elongation as they lack a 3’ OH

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6
Q

role of DNA helicase

A

unwinds DNA strand

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7
Q

what synthesised RNA primers

A

primase

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8
Q

describe the leading strand

A

DNA replicated 5’ to 3’ in one continuous strand

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9
Q

describe the lagging strand

A

DNA replicated 5’ to 3’ in short okazaki fragments which are later bound together

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10
Q

describe DNA polymerases role in proof reading

A

exonuclease activity - remove incorrect nucleotides

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11
Q

what are stem loops

A

regions of intra-molecular base pairing in DNA

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12
Q

what are the 3 classes of RNA

A
  • mRNA
  • tRNA
  • rRNA
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13
Q

what types of RNA are stable

A

tRNA and rRNA

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14
Q

describe mRNA

A

carries genetic information for protein synthesis

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15
Q

describe tRNA

A

carries amino acid to be incorporated into protein

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16
Q

describe rRNA

A

bnds with proteins to form ribosomes - site of protein synthesis

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17
Q

what is the 2D shape of tRNA

A

clover leaf

18
Q

anti-codon

A

triplet of bases that are complementary to a codon on the strand being replicated

19
Q

what are the 3 eukaryote RNA polymerases

A

Pol I, Pol II, Pol III

20
Q

what RNA polymerase synthesises all mRNA

A

Pol II

21
Q

give a brief overview of transcription

A
  • TATA box at -25 makes a kink in the DNA determining transcription start point and direction
  • general transcription factors are needed for initiation
  • transcription bubble moves along the DNA being unwound infrontof the polymerase and rewound behind it
  • new RNA strand creates a stem loop and a sequence of U bases to terminate transcription, mRNA is cleaved and DNA polymerase dissociates
22
Q

how is transcription regulated

A

by transcription factors binding to enhancers

23
Q

what are the 2 domains of transcription factors

A
  • DNA binding region

- transcription activated region

24
Q

describe how steroid receptors regulate transcription

A
  • steroid is activated and translocates to the nucleus where it binds to SREs on DNA and regulates transcription either -ve or +ve
25
Q

describe how glucocorticoid receptors regulate transcription

A
  • bound to albumin/transporter protein in blood and enter the cell via diffusion once free
  • binds to inactive steroid receptor in the cytoplasm and translocates to nucleus
  • binds to SRE
26
Q

what is at the ends of mRNA

A
  • 3’ - poly(A) tail

- 5’ - G cap

27
Q

give a brief overview of translation

A
  • initiation factors initiate (using GTP)
  • small ribosomal subunit binds to the 5’ end of mRNA and looks for a start codon
  • once found the initiator tRNA pairs at the P site and the large ribosomal subunit joins
  • elongation factors bring the next tRNA which binds at the A site, GTP hydrolysed, EF released
  • peptide bonds form between the P and A site - peptide in A
  • the free tRNA moves to the E site and exits (reused later)
  • the peptide is now in P and the A site is free for the next tRNA
  • once a stop codon is reached there is no tRNA pairinf and a release factor bonds in its place
  • GTP hydrolysed, protein cleaved and tRNA, mRNA and rRNA dissociate
28
Q

how is the genetic code degenerate

A

many amino acids have more than 1 codon

29
Q

how is the genetic code unambiguous

A

codons code for 1 amino acid or a stop

30
Q

function of amino-acyl tRNA synthases

A

binds amino acid to its corresponding tRNA (needs ATP)

31
Q

what catalyses peptide bond formation

A

peptidyl transferase

32
Q

what 3 things can happen after protein synthesis

A
  • modification
  • targeting
  • degradation
33
Q

modification

A

addition of chemical groups to proetin

34
Q

targeting

A

protein moved to final cellular destination

35
Q

degradation

A

unwanted/damaged proteins removed

36
Q

‘free’ ribosomes

  • are located where
  • make proteins for where
  • proteins are moved when
A
  • in cytosol
  • cytosol, nucleus, mitochondria
  • post-translationally
37
Q

‘bound’ ribosomes

  • are located where
  • make proteins for where
  • proteins are moved when
A
  • bound in rough ER
  • ER, golgi, secretions, plasma membrane
  • co-translationally
38
Q

types of post-translational modifications

A
  • glycolysation - addition of carbs in ER/golgi
  • formation of disulphide bridges
  • folding and assembly of multisubunits in ER
  • cleavage in ER, golgi or vesicles
39
Q

what is I-cell disease

A

inherited recessive disorder of protein targeting

- lysosomes are sorted right in the golgi and are secreted but unable to digest stuff

40
Q

what is a consequence of I-cell disease

A

early death