MGD Flashcards

0
Q

2 polar AA

A

Serine cysteine

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1
Q

3 non polar AA

A

Glycine alanine valine

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2
Q

2 negative AA and their general properties

A

Glutamate Aspartate acidic

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3
Q

2 positbe Aa and properties

A

Lysine Arginine basic

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4
Q

Type of Aa that are helix fixers and 2 examples

A

Small hydrophobic, ala leucine

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5
Q

Both helix breakers and why

A

Pro as no C-N rotation

Gly as R group supports other conformations

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6
Q

Initial clotting factor of intrinsic and extrinsic pathways

A

Intrinsic XI

Extrinsic III

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7
Q

first clotting factor in common

A

X

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8
Q

Describe from factor X onwards in clotting cascade

A

Prothrombin to thrombin (increases factor X concentration)
Fibrinogen to fibrin
Fibrin clot

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9
Q

How does glutamate take part in clotting cascade

A

Carboxyl action in the liver
Carboxyglutamate binds to Ca2+ and site damage
Ca2+ required for prothrombin cleavage

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10
Q

4 methods of controlling and stopping the clotting cascade

A

Localisation of Ca by carboxylglu
Digestion of factors by protein C once thrombin binds to endothelial receptors
Inhibitors eg anti thrombin III
Fibrinolysis

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11
Q

How many rings do purines have

A

2

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12
Q

What is DNA made from? Full name

A

Deoxy I mono phosphates dDNMPs

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13
Q

What is RNA made from?

A

NMPs

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14
Q

Stages of cell replication in order

A

M G1 S G2

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15
Q

Describe DNA replication

A

Origin of replication, helicase unwinds, primate adds primer, proteins recruit DNA polymerase

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16
Q

Name an X linked Dominant condition

A

X linked dominant hypophosphatemic rickets

17
Q

Prokaryotic origin of replication

A

Prinbow box

18
Q

Stop codons

A

UAA UAG UGA

19
Q

Two capping methods

A

Polyadenylation and 5’ to 5’ methyl guanine cap

20
Q

Translation

A

40S on 5’ cap and moves to methyl in P site
60s binds
Peptidyl transferase moves peptides between aminoacyltRNa
Translocation,
Finally peptide and tRNA is hydrolysed

21
Q

Lysosomal targeting enzymes

A

N acetyl glucosamine phospho transferase

N acetyl glucosamine phosphoglycosidase

22
Q

Mitcohondrial targeting

A

Amphipathic N terminal sequence, stabilised by MSF
Translocation by Tom Tim
Mitochondrial processing peptidase cleaves signal
Chaperones fold the protein

23
Q

Nuclear transport

A
NLS, binds to importin
Importin moves it into nucleus
Ran binds to importin and protein dislocates
Moves out of nucleus and dissociates
Ran moves back into nucleus
24
Q

ER targeting

A

SRPS, protein in via peptide translocation comples

25
Q

Tropocollagen

A

3 alpha RH chains
XY Gly
Pro to hydroxyl pro by prolyl hydroxylase ( vit C and Fe)
Cross links outside cell by Lysyl oxidase, between lysine residues

26
Q

Removal of pro collagen terminal peptidases

A

Pro collagen peptidase

27
Q

Penicillin

A

Inhibits trans peptidase enzyme, weak cell wall, lysis due to osmotic pressure

28
Q

Rifampcin

A

Binds to RNA polymerase

29
Q

Tetracycline

A

Competes with tRNA at A site

30
Q

SDS PAGE

A

Sodium do decal sulphate polyacylamide gel electrophoresis

31
Q

Southern blotting

A

DNA

32
Q

Array CGH

A

Array comparative genomic hybridisation
Entire genome of healthy and patient DNA in fragments
Where the DNA probe doesn’t bind to the patients then some mutation has occurred hence you can find its locus

33
Q

Transition

A

Purine to purine

34
Q

Trans version

A

Purine to pyrimadines

35
Q

5 causes of mutations

A
Tautomeric shift hence A to C, T to G
Slippage
Nitrous acid replacing amino groups with Keto groups
IQ disrupting packaging
UV causing adjacent thymine to bind
36
Q

Base exicion

A

1-5 bases, oxidative damage

37
Q

Nucleotide excision

A

Up to 30 bp replaced

38
Q

Short arm of chromosome

A

P

39
Q

Long arm of chromosome

A

Q

40
Q

DNA methylation

A

DNA is inactive

41
Q

Demethylation of DNA

A

Makes DNA acetyl groups hence it is active