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Folding (negative G) (Post-Translational modification(all 3 provide…

- - - - Ser
      - Thr
      - dual
    - - Ser/Thr
      - Tyr
      - dual
    - - WD40 bind pThr
  - - - stabilize secondary
    - - form tertiary from secondary
- - - - polar head group
        
        choline
        
        phosphate
        
        glycerol
        
        e.g. phospholipid head group PC, PE, PS, SM not a phospholipid, PI not abundant but can be phosphorylated and act as signaling molecule
        
        serine - +NH2 -COO-PO4=-1
        
        interior has strong (-) charge high PS
        
        choline - +N CH3..*3 -PO4=0
        
        ethanolamine - +NH3 -PO4=0
        
        sphingomyelin - NCH3..*3+PO4-=0
        
        inositol - not charged
      - two fatty acid tails
        
        14-24 carbon
        
        double bonds
        
        saturated tails straight and more flexible, double bond bends reduce flexibility and overall length
        
        free fatty acid (-)
    - - cell contact with envior or other cell
      - different sugar groups in many combinations
      - e.g.
        
        ceramide - basis of SM galactocerebroside
        
        Gal, not charged
        
        sialic acid (NANA) (-)
        
        GM1 ganglioside NANA (-)
    - - steroid ring, rigid
      - low lateral mobility, rotaion
      - polar hydroxyl group
    - - by vesicles (secretory pathway inbetween organelle)
      - carrierprotein through cytosol
      - contact site between organelles - ER, mito
      - cytosol
        
        nucleus (gated transport)
        
        peroxisomes过氧化物酶, mito, plastids 质粒体(tranmembrane transport
        
        ER-Golgi-late endosome-lysosome
        
        ER-Golgi-cell surface
        
        ER-Golgi-secretory vesicles-cell surface
        
        cell surface-early endo-late endo-Golgi-er
    - - on cytosolic side of ER mem
      - fatty acid(acyls) attach to coenzyme A
      - glycerol phosphate, head group added in sequence by enzyme
      - process
        
        fatty acid binding protein give fatty acid
        
        CoA transferase add CoA to fatty acid
        
        acyl transferase transfer glycerol 3 phosphate to fatty acid and remove CoA
        
        phosphatidic acid (PA) form
        
        phosphatase remove Pi o form diacylglycerol (DAG)
        
        choline phosphotransferase add CDP-choline to fatty acid CMP left with CMP, choline attach to fatty acid forming phosphatidyl choline
      - Coenzyme A
        
        carrier molecule ADP linker sulfhydryl
        
        reactive sulfhydryl
        
        adenine
        
        ribose
        
        fatty acyl CoA
        
        fatty acid transfer to glycerol phosphate in ER
        
        oxidative break down of fatty acid to acetyl in mito
        
        actyl CoA
        
        citric acid cycle oxidation in mito
        
        lysine acetylation
    - - phospholipid/cholesterol synthesize on cytosolic side of ER mem
      - scramblase protein flip lipid randomly (ATP-independent)-symmetric growth of both halves
        
        flippase proteins maintain membrane asymmetry
        
        ATP-dependent
        
        directional
        
        lipid-specific
      - transport through secretory pathway
  - - - thicker than surrounding membrane, rich in cholesterol
      - lipid with longer tails cluster together in rafts
      - cholesterol binding straightens lipid tails, causing thicker mebrane
- - - - sickle cell anemia, cystic fibrosis
  - - - insolubility
      - amyloid like aggregate, neurodegenerate
        
        Alzheimer, Parkinson, ALS 肝硬化
- - - - heat stress
        
        HS protein upregulated
        
        transcription of other protein down regulated
        
        response continue help cell recover
      - oxidative
      - proteasome inhibition
    - - domain
        
        DNA binding
        
        regulatory
        
        transcription activation
      - state
        
        inactive - monomeric
        
        active - trimer
        
        recognize heat shock element promoters
      - regulation
        
        mono HSF1 (folded) mimics unfolded
        
        bound by Hsp90
        
        heat shock
        
        unfolded protein compete with HSF1 for Hsp90
        
        free HSF1 trimerize, activate transcription
        
        chaperones (hsp90) express, help fold)
        
        HSF1 down regulated by binding of excess Hsp90 to monomer form
- - - - folding/trafficking chaperones
        
        native protein
        
        degradation (UPS)
      - remodelling (chaperones)
        
        misfolded
        
        degradation (chaperone)
      - aggregation
        
        amorphous aggregate, oligomers, amyloid fibrils
        
        autophagy/chaperones degredation
  - - - actively promote folding
        
        90
        
        bacteria, euka all
        
        70
        
        bacteria, euka cytosol, ER, mitoc
        
        chaperonins 60
        
        bacteria, archaea, euka cytosol, ER, mitochon
    - - prevent aggregation catalyze some folding steps
        
        calnexin protein disulfide isomerase
        
        euka ER
        
        peptidyl prolyl isoerase
        
        bacte, euka cyto, er, mito
        
        small HSP
        
        bac, cyto, er, mito
        
        prefoldin
        
        archaea, euka cyto