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Block II > Translation > Flashcards

Translation Flashcards

1
Q

How much of the genome encodes for protein?

A

A very small percent

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2
Q

What is the basic structure of amino acids

A

Backbone (amino and carboxyl group) and R group

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3
Q

What kind of bonds joins amino acids

A

covalent peptide

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4
Q

What makes AAs different from each other

A

The R group

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5
Q

What is the AA equivalent to the 5’ end

A

Amino (N) terminus

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6
Q

What is the AA equivalent to the 3’ end

A

Carboxy terminus

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7
Q

How many levels of protei structure are there

A

4

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8
Q

How many levels of structure do all proteins have

A

3

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9
Q

What are the levels of protein structure in order

A

Primary
Secondary
Tertiary
Quaternary

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10
Q

Describe primary protein structure

A

AAs covalently linked via peptide bonds

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11
Q

Describe the secondary protein structure

A

H-bonding of the peptide backbone causes peptide chain to fold into patterns
Alpha helices and beta sheets

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12
Q

Describe tertiary protein structure

A

Secondary elements organized into 3D stable units

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13
Q

What mediates and stabilizes tertiary protein structure

A

ionic and disulfide bonds between the amino acid side chains

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14
Q

Connection between hydrophobic AAs and tertiary structure

A

Tertiary structure allows them to be shielded from the aqueous environment

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15
Q

What is the name for structural units within a protein

A

Domains

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16
Q

Can a protein have more than one domain

A

Yes. Each has a uniques function

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17
Q

Do all proteins have quaternary structure?

A

No

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18
Q

What makes up the quaternary structure of a protein

A

Protein subunits (polypeptide)

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19
Q

What is the other name for quaternary structure

A

Oligomer

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20
Q

What are the segments of mRNA that code for each amino acid called

A

Codons

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21
Q

How many bases are in a codon

A

3

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22
Q

What is the start codon

A

AUG (codes for methionine)

23
Q

What determines the reading frame

A

The location of the start codon

24
Q

What are the stages of translation

A

Initiation
Elongation
Termination

25
Q

What direction does translation happen

A

5’-3’

26
Q

What are the ‘main players’ in translation

A

Ribosome
transfer RNAs (tRNAs)

27
Q

Ribosome-details

A

Large complex of protein and RNAs, 2 subunits
Moves along RNA and adds AAs

28
Q

tRNA details

A

Bind to RNA and AAs
One end has an anti-codon that binds to complementary mRNA codon and the other carries the corresponding amino acid

29
Q

What is an anticodon

A

Set of 3 nucleotides on a tRNA that bind to complementary mRNA codon

30
Q

Spark notes of initiation

A

Ribosome, mRNA, initiator tRNA combine to form initiation complex
Moves along RNA until start codon is reached

31
Q

Ribosome in initiation

A

Small subunit binds to mRNA 5’ cap
Once start codon is reached, large subunit joins

32
Q

tRNA in initiation

A

Binds to 5’ cap

33
Q

Spark notes of elongation

A

Polypeptide gets longer (surprise!)

34
Q

Ribosome in elongation

A

Exposes (A site) codons to rRNA, which attaches appropriate AAs (P site)
Peptide bond form with polypeptide chain and ribsome continues along mRNA

35
Q

Who recognizes stop codons

A

release factors (proteins)

36
Q

How do release factors work

A

make an enzyme that adds H2O to last molecule on polypeptide chain–no peptide bond –> protein chan separated from tRNA

37
Q

Why do proteins need chaperones

A

Because the environment is highly crowded and can be proteotoxic

38
Q

Chaperones:

A

proteins and protein complexes that enable successful protein folding

39
Q

How do chaperones work

A

Associate with proteins (usually hydrophobic sections) and suppress inappropriate reactions

40
Q

What are the two types of chaperones

A

Hsp60s and Hsp70s

41
Q

What are Hsp70s and how do they work

A

They are protein monomers. They bind to hydrophobic stretches

42
Q

What are Hsp60s and how do they work

A

Protein complexes. Provide and protected environment for protein folding

43
Q

Substitutions:

A

One base pair replaced with a different one

44
Q

What are the types of substitutions

A

Nonsense and missense

45
Q

Nonsense:

A

Stop codon coded for

46
Q

Missense:

A

Different AA coded for

47
Q

Insertion:

A

1 or more nucleotides added

48
Q

Deletion:

A

1 or more nucleotides removed

49
Q

What is a potential consequence of in-del mutations

A

Framshifts–triplet code is altered

50
Q

Therapeutic uses of protein chaperones

A

Low molecular weight molecules act like chaperones

51
Q

Types & functions of therapeutic chaperones

A

Chemical - nonspecific action (can work on many proteins)
Pharmacological - bind to specific proteins

52
Q

How can therapeutics be used to overcome premature stop codons?

A

Engineered suppressor tRNA reads premature stop codon as an AA

53
Q

What are the building blocks of proteins

A

Amino acids

Block II (28 decks)

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