Central Dogma & Enzymes Flashcards

1
Q

DNA → mRNA

A

Transcription

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2
Q

mRNA → Proteins/amino acids

A

Translation

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3
Q

What is the directionality of mRNA?

A

5’ Methyl cap → 3’ Poly A tail

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4
Q

Steps in Transcription:

A

1) Initiation
RNA polymerase attaches to promoter & TFIID shoots to start

2) Elongation
RNA polymerase moves along strand exposing 10-20 bases (THERE ARE MULTIPLE SITES)

3) Termination
2 types
Rho dependant
Rho-Indepenadant

4)Post transcriptional modifications
5’cap
3’Poly A tail
Splicing
Alternative splicing

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5
Q

Rho-dependant termination

A

P PROTEIN WEDGES

  • binds to mRNA transcript
  • moves reverse and eventually catches up to RNAPol to them stop it and kick itout
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6
Q

p protein

A

wedges in rho dependant termination

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7
Q

Rho- Indepenadant

A

HAIRPIN

  • RNA transcript fold back over self physically disrupting RNA path
  • rich in G and C but end stretch bunch of U
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8
Q

What are the post transcriptional modifications

A

pre mRNA → Mature mRNA

Add 5’ cap (methyl group)
Add 3’ poly A tail
Splice out introns
Alternative splice, remove certain exons to make proteins

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9
Q

Alternative splicing

A

remove certain exons to make proteins isoforms

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10
Q

Steps in Translation:

A

1) Inititation
- Small ribosomal subunit attaches to Methyl cap and slides to the start codon AUG
- tRNA with the anticodon for AUG binds to P site and brings in corresponding amino acids methionine

2) Elongation
- Another tRNA joins at the A site to then start the movement
- Methionine from previous amino acid attaches to this one and begins movement
- Shift and tRNA leaves after giving away it aminoacids

3) Termination
- When mRNA reaches stop codon tRNAs recognize it and bring in a release factor

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11
Q

Peptidyl transferase

A

Enzyme that catalyses the attachement/peptide bond making of amino acids

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12
Q

Post translational protein modifications

A

Covalent (EX. phosphorylation)
Cleavage/cutting

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13
Q

Histone

A

Protein that the DNA is wrapped around

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14
Q

Nucleosome

A

DNA wrapped around the histone

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15
Q

Purines

A

PURE AS GOLD(AG)

Adenine
Guanine

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16
Q

Pyrimidines

A

Thymine
Cytosine
Uracil

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17
Q

Nucleotide polymer (DNA backbone)

A
  • Back bone charge is negative
  • always labeled 5’ →3’
  • Made of: sugar, phosphate and base
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18
Q

DNA polymerase |||

A
  • Synthesizes new strand
  • On the leading strand
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19
Q

DNA polymerase |

A
  • removes primers on lagging strand and fills in the gaps
  • proof reads
  • removes primers and correlates mismatched pairs
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20
Q

how many H bonds do G-C have?

A

3

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21
Q

how many H bonds do A-T have?

A

2

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22
Q

DNA denaturing when…

A
  • pH less than 3 OR greater than 9
  • Heat to greater than 60 degrees (melting temp when half helical shape lost)
23
Q

DNA packaging. how are the proteins charged?

A

Basic proteins like Arg & Lys are positively charged and are. made to interact with negatively charged DNA

24
Q

Is DNA negatively or positively charged?

A

NEGATIVELY

25
Cofactors
INORGANIC EX. Zn 2+, Fe 2+
26
Coenzymes
ORGANIC EX. Vitamins
27
Holoenzyme
Active enzyme complex enzyme bound to cofactor or coenzyme
28
Apoenzyme
Enzyme alone is inactive
29
How do substrates bond to the acive site? 2 methods
NON COLVALENT interactions Lock in key method Induced fit model
30
Lock in key method
Perfect fit
31
Induced fit model
Overtime gradually shapes into fit better
32
Enzyme related diseases: TISSUE DAMAGE
elevated enzyme presence in plasma (out of cells)
33
Enzyme related diseases: LIVER DISEASE
ALT= liver enzyme if found in blood liver is damaged
34
Enzyme related diseases: HEART DISEASE
Cardiac enzymes could be found in plasma. that way can find out if heart is damaged
35
Exergonic
less energy left as opposed to when we started
36
Endergonic
more energy left as opposed to when we started
37
what does it mean when DELTA G is 0?
Equilibrium
38
Michaelis-Menton Model
Model to described catylized enzyme reactions (NOT allosteric enzymes)
39
What shape is the Michaelis-Menton Model?
Rectangular porabola
40
Km=
A suubstrate [ ] that tells us how much substrate is required to get to half Vmax.
41
HIGH Km
Low affinity for substrate
42
LOW Km
High affinity for substrate
43
Lineweaver Burke EQ
Double reciprocal of Michaelis-Menton EQ (both sides put 1 over)
44
Environmental factors affecting enzyme activity
pH EX. Stomach enzymes work better in stomach acid pH Temperature EX. enzymes work faster at high temp but at a certain point denature because too hot
45
Cold blooded animals in the cold
move slow because enzymes move slow
46
Hydrothermal Vents have Thermopiles aquaticus
animals that love the heat so their enzymes work better in hot
47
Siamese cats
Pigmentation enzyme is sensitive to heat and denature sat cats body temp So only the cold parts of the cat are pigmented like nose and paws
48
Alosteric enzymes
Sigmoidal curve have the little indent
49
Alosteric regulators (name and 2 types)
Effectors: Homotropic Heteroptropic
50
Homotropic effectors
Substrate changes shape and goes into alosteric site to ACTIVATE
51
Heterotropic effectors
Foreign molecule comes into allosteric site and either INHBITS OR ACTIVATES
52
Covalent modification of an enzyme (EX and difference between allosteric regulation)
EX. Phosphorelation Takes longer because need other reactions involved
53
Positive regulator: what it does? whch way shift?
helps make more Shift left
54
Negative regulator: what it does? whch way shift?
stops production Shift right