Protein and structure

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  • 8 Protein Structure and Function
    • Different mechanisms of protein self assembly
      • Assembly on core, accumulated stain, vernier mechanism
      • e.g. viral capsizes self assemble from identical monomers, tobacco mosaic virus (TMV) assembles around an RNA core
      • Interactions require complementary surfaces
        • 1) Surface - string, 2) Surface - surface 3) Helix - helix
    • Further interactions
      • Hydrophobic interactions drive coiled-coil packaging
      • Tubulin subunits that make up microtubules can pack into a variety of structures; filaments, sheets, rings, tubes
      • Lipid membrane hydrophobic and so must proteins that cross it
        • Single pass, multiples, B-barrel (pore), amphipathic helix
        • Hydropathy plots can show which parts of transmembrane proteins are hydrophobic
    • Lipid modifications
      • A variety of lipophilic covalent attachementsthat help to bind proteins to membranes
        • Inside; acylation or prenylation
        • Outside; GPI anchors (a simple sugar and a phospholipid)
    • Carbohydrate modification (glycosylation)
      • Modification of extra-cellular proteins
      • Two types; N linked (attached via asparagine) or o-linked (attached via hydroxyl group of serine, threonine or hydroxycysteine
      • Gives cellular protection; mucins in mucous
      • Provides adhesive properties; sticky
      • Provides a varied and complex set of surfaces for interactions
    • Phosphorylation and dephospho rylation
      • Majour secondary and regulatory modification. No intrinsic.
      • Protein kinases (Src) - acts as a switch. Converts a hydroxyl group to a bulky charged phosphate group.
    • Proteins as molecular motors
      • ATP dependent movement along a track. (Myosin in actin, kinesin in microtubules,polymerases on DNA)


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