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IB Bio Y1 HL > T7.3 Translation HL > Flashcards

T7.3 Translation HL Flashcards

1
Q

Activation of tRNA molecule involves attaching what to the 3’terminal tRNA?

A

appropriate amino acid

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2
Q

How many different tRNA-activating enzymes are there?

A

20, 1 for each amino acid

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3
Q

Is ATP require for activation of tRNA?

A

yep

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4
Q

Step 1 of activation of tRNA

A

correct amino acid binds to the correct amino-acetyl tRNA synthase (activating enzyme)

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5
Q

Step 2 of tRNA activation

A

ATP binds to amino-acetyl tRNA synthase (activating enzyme)

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6
Q

Step 3 of tRNA activation

A

Amino acid is activated (ready for the tRNA) by the covalent binding of ATP

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7
Q

Step 4 of tRNA activation

A

Phosphate is released from ATP, making AMP (ATP but 1 phosphate group)

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8
Q

Step 5 of tRNA activation

A

Correct tRNA binds to the synthethase

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9
Q

Step 6 of tRNA activation

A

Amino acid is attached to the tRNA through covalent bonds.

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10
Q

Step 7 of tRNA activation

A

AMP is released

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11
Q

Step 8 of tRNA activation

A

the activated/charged tRNA leaves the amino-acetyl tRNA synthase

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12
Q

What is amino-acetyl tRNA synthase?

A

The enzyme that activates tRNA, “looks like an earwax thing” - mrs austin

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13
Q

Function of Site A on a ribsome

A

Holds tRNA that carries the next amino acid
(Acceptor)

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14
Q

Function of Site P on a ribsome

A

Holds tRNA with the growing polypeptide chain
(Peptidyl)

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15
Q

Function of Site E on a ribsome

A

site where tRNA that lost its amino acid is discharged
(exit)

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16
Q

Step 1 of intitation of translation

A

mRNA binds to small subunit

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17
Q

Step 2 of intitation of translation

A

Initiator tRNA molecule carrying methionine binds to the start codon AUG

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18
Q

What is the start codon for translation?

A

AUG, carries methionine

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19
Q

Step 3 of intitation of translation

A

large ribosomal subunit binds to small subunit

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20
Q

Step 4 of intitation of translation

A

Initiator tRNA is in the P site

21
Q

Step 5 of intitation of translation

A

Next codon signals another tRNA occupying A site

22
Q

Step 6 of intitation of translation

A

Peptide bond is formed between the amino acids in the P and A site

23
Q

What is elongation in translation?

A

The continued synthesis of a polypeptide after initiation

24
Q

Step 1 of Elongation in translation

A

The ribosome translocates 3 bases (1 codon) in the 5’-3’ direction down the mRNA

25
Q

Step 2 of Elongation in translation

A

tRNA in P moves to E

26
Q

Step 3 of Elongation in translation

A

tRNA in E leaves

27
Q

Step 4 of Elongation in translation

A

tRNA in A moves to P

28
Q

Step 5 of Elongation in translation

A

A tRNA with an appropriate anticodon occupies the vacant A site

29
Q

Step 6 of Elongation in translation

A

next amino acid is added to gorwing peptide chain by condensation reaction, forming a peptide bond

30
Q

Termination of Translation

A

Process continues until stop codon is reached.
Polypeptide released

31
Q

Free ribosome’s proteins go where?

A

the proteins are used inside the cell

32
Q

Bound ribosome’s proteins go where?

A

outside of the cell (secreted) or for use in lysosomes

33
Q

What determines whether a ribosome will be free or bound?

A

The prescene of signal sequences means a ribsome will be bound

34
Q

Signal sequence

A

sequence of amino acids at the beginning of the polypeptide.
Binds to the signal recognition protein and allows for the polypeptide to enter ER

35
Q

Differences between eukaryotic and prokaryotic translation/transcription

A

Eukaryotes have nuclear compartmentalization, which causes a delay between transcription and translation. Prokaryotes do not have this delay and have no compartmentalization.

36
Q

Polysome

A

multiple ribosomes translating a strand of mRNA, produces multiples of the sam polypeptide.

37
Q

Are polysomes in prokaryotes or eukaryotes

A

theyre in both bro

38
Q

Primary structure of proteins

A

just the sequence of amino acids in the protein chain

39
Q

Secondary structure of protiens

A

the structures created by formation of hydrogen bonds between COOH and NH (alpha helix or beta pleated sheet)

40
Q

Can u identify an alpha helix??

A

u better
like curls and twisty

41
Q

Can u identify beta pleated sheets??

A

u better
the flat and not curly one, sometimes with arrow on it

42
Q

Tertiary structure

A

the further folding of the polypeptide stabilized by interactions between R groups
overall 3D shape

43
Q

How do covalent bonds effect the tertiary structure?

A

the covalent bonds are used to form disulfide bridges

44
Q

How do hydrogen bonds effect the tertiary structure of proteins?

A

form between thee polar groups (NH3 and COOH), and folds it more

45
Q

How does Van deer Waals effect the tertiary structure of proteins?

A

makes the hydrophobic groups inward and hydrophobic groups outward, and vice versa

46
Q

How do ionic bonds effect the tertiary structure of proteins?

A

Form between positively charged atoms/molecules to negatively charged atoms/molecules to effect the shape

47
Q

Quaternary structure

A

Exists in proteins with more than one polypeptide chain.
These chains combine to form a single structure
Not all proteins have this structure
All bonds mentioned before are involved

48
Q

Prostheic group

A

A non-polypeptide group in the protein
Ex: Hemoglobin, heme group is involved which is iron

IB Bio Y1 HL (27 decks)

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