Translation

Question 1

How much of the genome encodes for protein?

Answer 1

A very small percent

Question 2

What is the basic structure of amino acids

Answer 2

Backbone (amino and carboxyl group) and R group

Question 3

What kind of bonds joins amino acids

Answer 3

covalent peptide

Question 4

What makes AAs different from each other

Answer 4

The R group

Question 5

What is the AA equivalent to the 5’ end

Answer 5

Amino (N) terminus

Question 6

What is the AA equivalent to the 3’ end

Answer 6

Carboxy terminus

Question 7

How many levels of protei structure are there

Answer 7

4

Question 8

How many levels of structure do all proteins have

Answer 8

3

Question 9

What are the levels of protein structure in order

Answer 9

Primary
Secondary
Tertiary
Quaternary

Question 10

Describe primary protein structure

Answer 10

AAs covalently linked via peptide bonds

Question 11

Describe the secondary protein structure

Answer 11

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

Question 12

Describe tertiary protein structure

Answer 12

Secondary elements organized into 3D stable units

Question 13

What mediates and stabilizes tertiary protein structure

Answer 13

ionic and disulfide bonds between the amino acid side chains

Question 14

Connection between hydrophobic AAs and tertiary structure

Answer 14

Tertiary structure allows them to be shielded from the aqueous environment

Question 15

What is the name for structural units within a protein

Answer 15

Domains

Question 16

Can a protein have more than one domain

Answer 16

Yes. Each has a uniques function

Question 17

Do all proteins have quaternary structure?

Answer 17

No

Question 18

What makes up the quaternary structure of a protein

Answer 18

Protein subunits (polypeptide)

Question 19

What is the other name for quaternary structure

Answer 19

Oligomer

Question 20

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

Answer 20

Codons

Question 21

How many bases are in a codon

Answer 21

3

Question 22

What is the start codon

Answer 22

AUG (codes for methionine)

Question 23

What determines the reading frame

Answer 23

The location of the start codon

Question 24

What are the stages of translation

Answer 24

Initiation
Elongation
Termination

Question 25

What direction does translation happen

Answer 25

5'-3'

Question 26

What are the 'main players' in translation

Answer 26

Ribosome transfer RNAs (tRNAs)

Question 27

Ribosome-details

Answer 27

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

Question 28

tRNA details

Answer 28

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

Question 29

What is an anticodon

Answer 29

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

Question 30

Spark notes of initiation

Answer 30

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

Question 31

Ribosome in initiation

Answer 31

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

Question 32

tRNA in initiation

Answer 32

Binds to 5' cap

Question 33

Spark notes of elongation

Answer 33

Polypeptide gets longer (surprise!)

Question 34

Ribosome in elongation

Answer 34

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

Question 35

Who recognizes stop codons

Answer 35

release factors (proteins)

Question 36

How do release factors work

Answer 36

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

Question 37

Why do proteins need chaperones

Answer 37

Because the environment is highly crowded and can be proteotoxic

Question 38

Chaperones:

Answer 38

proteins and protein complexes that enable successful protein folding

Question 39

How do chaperones work

Answer 39

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

Question 40

What are the two types of chaperones

Answer 40

Hsp60s and Hsp70s

Question 41

What are Hsp70s and how do they work

Answer 41

They are protein monomers. They bind to hydrophobic stretches

Question 42

What are Hsp60s and how do they work

Answer 42

Protein complexes. Provide and protected environment for protein folding

Question 43

Substitutions:

Answer 43

One base pair replaced with a different one

Question 44

What are the types of substitutions

Answer 44

Nonsense and missense

Question 45

Nonsense:

Answer 45

Stop codon coded for

Question 46

Missense:

Answer 46

Different AA coded for

Question 47

Insertion:

Answer 47

1 or more nucleotides added

Question 48

Deletion:

Answer 48

1 or more nucleotides removed

Question 49

What is a potential consequence of in-del mutations

Answer 49

Framshifts--triplet code is altered

Question 50

Therapeutic uses of protein chaperones

Answer 50

Low molecular weight molecules act like chaperones

Question 51

Types & functions of therapeutic chaperones

Answer 51

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

Question 52

How can therapeutics be used to overcome premature stop codons?

Answer 52

Engineered suppressor tRNA reads premature stop codon as an AA

Question 53

What are the building blocks of proteins

Answer 53

Amino acids