Protein structure

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  • Protein Structure
    • Folding of a peptide into a protein
      • Hydrophobic core region contains non-polar side chains. Polar side chains on outside can form hydrogen bonds with water. This can drive folding
      • Held together by interactions; ionic (attraction between +ve and -ve), van der Walhs, electrical (attraction and repulsion), hydrogen bonds (involves O and N atoms forming a charge cloud)
      • Primary structure read from left to right
    • Secondary Structure
      • a-helix, b-sheet, random coil
      • 7 amino acids per 2 turns in an a-helix (heptaoid), intra-chain H bond runs vertically every 4th residue
      • Interchain H bonds between b-sheets. Anti-parallel B-sheets have B-turns, parallel have long loops
    • Random coil
      • Everything between a-helix and b-sheet
    • Tertiary Structure
      • The way in which secondary structures pack together
      • Src tyrosine kinase - a multidomain soluble protein (made of 4 functional domains)
    • Quaternary Structure
      • Relationship between individual proteins in a multimeric complex
    • Post - translational modifications
      • Disulphide bonds, proteolysis, glycosylsation, lipid modification, phosphorylation/ dephosophorylation
        • Disulphide bonds typically found in proteins exposed to extremes of environment (conditions variable) e.g enzymes
        • Proteolytic processing of precursor protein
          • Active hormone or enzyme cleaved to yield a mature functional molecule


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