Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

BIO 202 > Protein translation > Flashcards

Protein translation Flashcards

1
Q

Transcription

A

DNA–> RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Translation

A

mRNA–> Protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What do tRNAs do?

A

The adaptor molecule between amino acid and anticodon sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What do tRNA synthetase’s do?

A

The enzyme that creates the high energy bond between amino acid and tRNA, takes 2 P off of ATP and creates AMP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What can the energy in the tRNA:amino acid bond do?

A

create peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are ribosomes composed of?

A

Proteins and RNAs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Describe where the enzymatic subunit, the amino acids and the anticodon loop are in the ribosome?

A

The enzymatic subunit is between the P and the A site, the anticodon loop is in the bottom closer to the small subunit, the amino acids are at the top of the subunit

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are the E, P and A sites on the ribosomes?

A

Aminoacyl, peptidyl and exit site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Where is the 5’ cap and why is it included?

A

Stability, created because there is a portion of mRNA before the start codon that is not translated,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

3’ Poly-A-tail, what is it? Function?

A

Makes it more stable, interacts with 5 end protein cap and makes the molecule more stable before it is translated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How does initiation begin?

A

Small subunit attacks at the 5’ end, it contains a MET tRNA already and has Elf 2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the elf-2?

A

Elongation factor, it attaches MET

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

step 2 of translation initiation

A

SRU slides along until it reaches the start codon , then it will hydrolyze GTP–>GDP and then release elf2 which was blocking the large subunit

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is the purpose of adding phosphetase on Serine, threonine, tyrosine?

A

Assembly of protein into larger complex

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What type of modification is phosphorylation?

A

post-translational

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Why is phosphorylation common on threonine, tyrosine and serine?

A

They all contain a free OH group where PO4 can be added

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What type of modifications can occur to proteins?

A

Nucleotide regulation, covalent modification,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Function of hydrolase?

A

catalyze breakage of covalent bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Protease function?

A

digesting/cleaving, breaks 2 amino acids apart

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Isomerase

A

rearrange things/bonds in a single molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Kinase function

A

attach phosphate to molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Phosphotase

A

remove phosphate from a molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What do enzymes do?

A

Decrease the energy of a rxn, (activation energy) so that a chemical rxn is biochemically relevant, or bring substrates closer together, or put physical strain on a molecule to bring substrates together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Negative enzyme regulation

A

End product stops earlier enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Positive enzyme regulation
product activates next steps
26
What does phosphorylation do?
Phosphorylation can turn a protein on or off by adding PO4
27
What is nucleotide regulation?
noncovalent interaction in which a protein will bing to GTP, then the 3rd phosphate is taken off, GDP, and turned on
28
what is a GEF?
Guana nucleotide exchange factor in which exchanges GDP to GTP
29
What plays a GEF role in translation elongation?
EF-Ts- binds to EFTU and brings in GTP in exchange for GDP
30
What is a GAP?
GTPase inactivating protein that removes the P from GTP and makes GDP, turns GTPase off
31
GTP hydrolysis as a role in elongation factors
GTP with elongation factors, there are 3 domains, when GTP is bound 2 of them are together and the GTP interacts with the switch helix, this pulls the third in and created a binding pocket. When it is hydrolyzed the GDP is shorter and can't interact with the switch helix
32
ATP hydrolysis in proteins
This can produce a mechanical force and changes shape, shifting the protein. Can facilitate transport across a membrane
33
What blocks the large subunit from binding to a protein being translated and why?
ELF-2, blocks the large subunit until the small subunit reaches a start codon
34
What is translation elongation?
Cyclical and progressive movement,
35
How does translation elongation work?
When the correct tRNA is matched, GTP is hydrolyzed, then the switch helix cannot interact. tRNA is detached. then the 2 subunits can't interact
36
How does EFTU assist with translation?
elongation, it is bound to other tRNAs (not first) once correct tRNA is placed, it releases and an enzymatic process begins with the large subunit, the large subunit shifts over, then EFG binds in the 1 and 2 site, GTP--> GDP then the small subunit shifts over
37
What begins translation termination?
Release factors bind to the A site, they contain side chains that bind to the stop codon and facilitate a rxn between tRNA and protein. Then subunit falls apart
38
Dissociation process
Side chain interacts with ribosomes and tRNA, (detaches tRNA and C-terminus), 3 release factors
39
What are actin filaments?
Helical polymers of protein actin, they contain a +/- end, also contain stress factors that reinforce structure of cytoskeleton
40
Structure of actin filaments
Built from actin monomers, they are bound to ATP when floating, when in a filament, they can be hydrolyzed to ADP
41
What is actin polymerization? | 3 steps
Nucleation, elongation and steady state
42
Nucleation of actin polymerization
Small cluster of actin forms
43
Elongation of actin polymerization
Rapid addition of actin monomers occurs, plus end adds faster
44
Steady state of actin polymerization
Over time, actin filaments reach a steady state where the rate of monomer addition at the barbed end equals the rate of monomer dissociation at the pointed end.
45
Treadmilling
when the rt of addition at the plus end equals the rate of dissociation on the minus end
46
What domain do proteins that associate with actin commonly have?
SH domain
47
Profilin
Profilin promotes actin formation
48
What is Thymosin?
binds to actin monomers, blocking the binding pocket, this makes the + end unable to grow
49
What is Arp 2/3?
Arp 2/3 is a protein complex that mimics the shape of the + end. First binds to a preformed actin filament, then actin monomers will add to the + end (branching)
50
How does branching occur
Arp 2/3 rapidly adds to its own end while attached to a preformed actin filament
51
What is formin?
Formin interacts with the + end, forms a ring that rocks back and forth, protecting the end. Contains domains that have binding sites for profilin(addd)
52
What are capping proteins?
Interact with the + or - end, block addition or subtraction of monomers,
53
What is cofilin?
Cofilin mediates disassembly through twisting of actin filament
54
What are actin-cross-linking proteins?
interact alongside of actin with SH domains, alpha-actinin or fimbrins
55
What is fimbrin?
2 SH domains that are close together, actin binds to them and creates tight actin bundles. Motor proteins cannot penetrate
56
What is alpha actinin?
2 SH domains with protein complexes in the center, holds actin filaments apart - motor proteins and myosin can enter
57
What is filopodium in a migrating cell?
Filopodium are tight parallel bundles created by fimbrin
58
What is lamellipodium?
Dendritic network created by Arp 2/3
59
What is the cell cortex in a migrating cell?
Gel like network, contains filamin
60
What are stress fibers in a migrating cell?
Contain alpha actinin
61
What are myosins?
Motor proteins that bind to ATP, they walk along or pull actin filaments
62
What is the structure of myosins?
4 subunits, 2 light, 2 dark chain
63
What are the 4 steps of protein movement?
Attached, released, cocked, force-generating
64
What occurs at the attached step of protein movement?
The myosin head is attached firmly to the actin filament at the binding pocket
65
What step occurs at the release step of protein movement?
ATP attacks the binding pocket, disrupts the pocket and releases it from the actin filament
66
What happens at the cocked stage of protein movement?
The lever arm extends, bc of breakage of the phosphate bond
67
What happens at the force-generating step of protein movement?
P is released, triggers power-stroke, regains OG shape and ATP comes back
68
What is light chain phosphorylation?
Myosin LCK uses ATP to phosphorylate the light chain and activate the protein
69
MLCP
turns off the light chain by removing an ATP
70
What are Microtubules made up of?
alpha and beta tubulin dimers, both are bound to GTP
71
Which end in microtubules is dynamic?
The beta (+) end
72
What is microtubule assembly dependent on?
the gamma tubulin ring
73
What are protofilaments made up of? And what do they make up?
Protofilaments make up microtubules, they are made up of alpha and beta dimers
74
Explain the dynamics of microtubules
Microtubules have rapid growth at the B (+) end, GTP is attached, when the subunits interact, it turns into GDP, if the GDP catches up to the GTP, Catastrophe occurs, rapid loss occurs, then Rescue occurs if GTP subunits are added back on
75
How do protofilaments align when GTP is bound?
They align in a straight line, providing stability
76
What interactions keep protofilaments stable?
Protofilaments horizontally interact with noncovalent bonds
77
What are microtubule organizing centers made out of?
Centrosomes, a mother and daughter pair of centrioles that are made of 9 triplet microtubules
78
What does the mother centriole have/do in microtubule organizing centers?
Has distal appendages, recruits pericentriolar material (protein dense), and organizing structures made of 9 triplet microtubules
79
What are central spokes made up of in microtubule organizing centers?
SAS 6 forms dimers, 9 of them line up, then triplet microtubules are recruited
80
What is the Gamma tubulin small complex?
each has 2 gamma tubulin, 7 total come together to make a ring, in a lock washer spiral (1st and last overlap)
81
How do 13 gamma tubulins connect to something else with 13?
There are 13 protofilaments in which they connect at
82
What are the MAPS we learned about?
Catastrophe factor, XMAP 215, Statnmin, katanin, MAP2, TAU
83
What does Catastrophe factor do?
kinesin 13, grabs at + end and curves outward
84
What does XMAP 215 do?
Binds to tubulin dimer, brings in and prevents outward curving
85
What is statnmin?
Protein that associates with 2 dimers stuck together, then associates with + end, curves outward and prevents reattachment
86
What is katanin?
Katanin slices microtubules, assembles specialized structures at middle, grabs on and unwinds, can also just break off from organizing center
87
What is MAP2 and what type of cells does it work with?
MAP 2 works with neurons. In the axons, provides rigid spacing to support outgrowth, has microtubule bonding domain and spacing domain that branches off at 90 degrees
88
What are + tip proteins
associates with end of + side of microtubules. Link + end to other things, different organelles, etc
89
What is TAU?
MAP that helps with spacing in neurons, has larger angle than MAP2 and shorter distances apart
90
What are Kinesins?
+ end motor proteins, walk towards the + end, kinesin 1 is the major cargo carrier
91
How do Kinesins move?
ATP--> ADP hydrolysis cycle, 1. lagging head is attached to ATP, leading head is attached to ADP 2. Lagging head hydrolyzes ATP--> ADP, releases and changes how the binding occurs (binding pocket) 3. Phosphate releases from lagging head, ADP--> ATP, then, the heads line up 4. heads switch places
92
What are Dyneins?
- end motor proteins, more complex and have microtubule binding domain, not as stable as kinesins
93
What is cytoplasmic dynein transport?
Associated with dynactin complex
94

BIO 202 (3 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions