MGD Flashcards
2 polar AA
Serine cysteine
3 non polar AA
Glycine alanine valine
2 negative AA and their general properties
Glutamate Aspartate acidic
2 positbe Aa and properties
Lysine Arginine basic
Type of Aa that are helix fixers and 2 examples
Small hydrophobic, ala leucine
Both helix breakers and why
Pro as no C-N rotation
Gly as R group supports other conformations
Initial clotting factor of intrinsic and extrinsic pathways
Intrinsic XI
Extrinsic III
first clotting factor in common
X
Describe from factor X onwards in clotting cascade
Prothrombin to thrombin (increases factor X concentration)
Fibrinogen to fibrin
Fibrin clot
How does glutamate take part in clotting cascade
Carboxyl action in the liver
Carboxyglutamate binds to Ca2+ and site damage
Ca2+ required for prothrombin cleavage
4 methods of controlling and stopping the clotting cascade
Localisation of Ca by carboxylglu
Digestion of factors by protein C once thrombin binds to endothelial receptors
Inhibitors eg anti thrombin III
Fibrinolysis
How many rings do purines have
2
What is DNA made from? Full name
Deoxy I mono phosphates dDNMPs
What is RNA made from?
NMPs
Stages of cell replication in order
M G1 S G2
Describe DNA replication
Origin of replication, helicase unwinds, primate adds primer, proteins recruit DNA polymerase
Name an X linked Dominant condition
X linked dominant hypophosphatemic rickets
Prokaryotic origin of replication
Prinbow box
Stop codons
UAA UAG UGA
Two capping methods
Polyadenylation and 5’ to 5’ methyl guanine cap
Translation
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
Lysosomal targeting enzymes
N acetyl glucosamine phospho transferase
N acetyl glucosamine phosphoglycosidase
Mitcohondrial targeting
Amphipathic N terminal sequence, stabilised by MSF
Translocation by Tom Tim
Mitochondrial processing peptidase cleaves signal
Chaperones fold the protein
Nuclear transport
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
ER targeting
SRPS, protein in via peptide translocation comples
Tropocollagen
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
Removal of pro collagen terminal peptidases
Pro collagen peptidase
Penicillin
Inhibits trans peptidase enzyme, weak cell wall, lysis due to osmotic pressure
Rifampcin
Binds to RNA polymerase
Tetracycline
Competes with tRNA at A site
SDS PAGE
Sodium do decal sulphate polyacylamide gel electrophoresis
Southern blotting
DNA
Array CGH
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
Transition
Purine to purine
Trans version
Purine to pyrimadines
5 causes of mutations
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
Base exicion
1-5 bases, oxidative damage
Nucleotide excision
Up to 30 bp replaced
Short arm of chromosome
P
Long arm of chromosome
Q
DNA methylation
DNA is inactive
Demethylation of DNA
Makes DNA acetyl groups hence it is active
