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36 Cards in this Set
- Front
- Back
Acylation |
is the process of adding an acyl group to a compound. |
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What enzyme is responsible for acylation |
acetyl transferases |
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Ex. of Acylation |
chymotrypsin ping pong mechanism: acylation and deacylation |
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acylation of lysine is important for what |
regulation of gene expression, localization, and enzymatic activity |
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Biotinylation catalyzed by what |
* biotin protein ligase
* BIOTIN + ATP-> BIOTINOYL-AMP + Apo Domain->(AMP leaves) holo domain biotinylated protein |
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Glcosylation |
* important for cell-cell communication
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oxidation of _________ is associated with oxidative stress and aging |
methionine |
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Oxidation of methionine can affect what protein? and how? |
calmodulin, inactivation of calmodulin |
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Calmodulin (CaM) |
* calcium-modulated protein
* binds to CALCIUM- and CaM SQUISHES TOGETHER * Squished CaM binds to ATPase * ATPase can now produce ATP= release of inhibition |
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What happens when methionine in CaM is oxidized? |
* CaM cannot squish together when Calcium binds- bc methionine helix STIFF
* CaM doesn't release inhibition of ATPase, and ATP is NOT produced |
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oxidation of ________ can be a growth factor induced signal to ramp up cellproliferation via phosphorylation of Tyrosine. and how does it do this? |
cystein, formation of disulphide bonds |
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gluthionylation |
oxidation of Cystein |
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What does the mixed disulfine cystein do? |
controls levels of disulfide bonding |
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What is the most important PTM? and what does it do... |
phosphorylation, signal transduction, mediatingenzyme activity, protein interactions |
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What are the enzymes involved in phosphorylation |
protein kinases: add P's phosphatases: remove P's |
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Phosphatase targets |
1. amino acids
2. protein domains 3. non-specific |
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MAPK |
* phosphorylate serine and tyrosine (both polar a.a)
* STAT dimerization to activate gene expression |
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peptide bond |
condensation reaction (removal of h2O) in ribosome |
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first protein to be sequenced... by whom? |
insulin, sanger |
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mulder |
whats in the protein..elemental analysis |
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peptides can do what |
1. hormones: ex. insulin, oxytocin
2. neuropeptides: ex. somatostatin |
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Acyltrasferases |
metabolic control by acylation: inhibition, activation, competition |
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Acyltrasferase inhibition |
blocking access to motif |
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Acyltrasferases activation |
allowing access to phosphoserine |
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Acyltrasferases competition |
competing to prevent other modifications |
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biotynylation is important for what |
regulating gene expression,fatty acid metabolism, and neurogenesis |
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peptide poisons |
1. Pro-Tx1 (spider venom)
2. Muscarinic Toxin 3. Conotoxins 4. Snake venom toxins |
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ProTx-1 |
irrevesibly binds to ion gated channels |
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muscarinic toxin 3 |
brain toxin- motor control memory |
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conotoxins |
inhibit acetylcholine receptors in nerves and muscles, sodium channels, potassium channels |
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snake venoms |
interfere with * phosphodiesterase: bld pressure drops * cholinesterase: loss of muscle control |
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phi bond |
N-C bond |
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psi |
C-CO bond remember: PSSSSI <-> C-C bond |
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Ramacharan |
top left: Beta and poly P top right: alpha Left handed bottom right: alpha |
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Glycine and Ramacharan |
the only residue without a C atom, is much less sterically hinderedthan the other amino acid residues. Hence, its permissible rangeof and covers a larger area of the Ramachandran diagram. |
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secondary structure of protein |
H-bonds |