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
Q

Cofactors

A

INORGANIC
EX. Zn 2+, Fe 2+

26
Q

Coenzymes

A

ORGANIC
EX. Vitamins

27
Q

Holoenzyme

A

Active enzyme complex
enzyme bound to cofactor or coenzyme

28
Q

Apoenzyme

A

Enzyme alone is inactive

29
Q

How do substrates bond to the acive site?
2 methods

A

NON COLVALENT interactions
Lock in key method
Induced fit model

30
Q

Lock in key method

A

Perfect fit

31
Q

Induced fit model

A

Overtime gradually shapes into fit better

32
Q

Enzyme related diseases: TISSUE DAMAGE

A

elevated enzyme presence in plasma (out of cells)

33
Q

Enzyme related diseases: LIVER DISEASE

A

ALT= liver enzyme
if found in blood liver is damaged

34
Q

Enzyme related diseases: HEART DISEASE

A

Cardiac enzymes could be found in plasma. that way can find out if heart is damaged

35
Q

Exergonic

A

less energy left as opposed to when we started

36
Q

Endergonic

A

more energy left as opposed to when we started

37
Q

what does it mean when DELTA G is 0?

A

Equilibrium

38
Q

Michaelis-Menton Model

A

Model to described catylized enzyme reactions (NOT allosteric enzymes)

39
Q

What shape is the Michaelis-Menton Model?

A

Rectangular porabola

40
Q

Km=

A

A suubstrate [ ] that tells us how much substrate is required to get to half Vmax.

41
Q

HIGH Km

A

Low affinity for substrate

42
Q

LOW Km

A

High affinity for substrate

43
Q

Lineweaver Burke EQ

A

Double reciprocal of Michaelis-Menton EQ (both sides put 1 over)

44
Q

Environmental factors affecting enzyme activity

A

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
Q

Cold blooded animals in the cold

A

move slow because enzymes move slow

46
Q

Hydrothermal Vents have Thermopiles aquaticus

A

animals that love the heat so their enzymes work better in hot

47
Q

Siamese cats

A

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
Q

Alosteric enzymes

A

Sigmoidal curve
have the little indent

49
Q

Alosteric regulators (name and 2 types)

A

Effectors:
Homotropic
Heteroptropic

50
Q

Homotropic effectors

A

Substrate changes shape and goes into alosteric site to ACTIVATE

51
Q

Heterotropic effectors

A

Foreign molecule comes into allosteric site and either INHBITS OR ACTIVATES

52
Q

Covalent modification of an enzyme (EX and difference between allosteric regulation)

A

EX. Phosphorelation
Takes longer because need other reactions involved

53
Q

Positive regulator:
what it does?
whch way shift?

A

helps make more
Shift left

54
Q

Negative regulator:
what it does?
whch way shift?

A

stops production
Shift right