Protein Topic- Mindmap

Comprehensive, detailed mindmap for the topic of Proteins in AS biology. I follow the CCEA specification.

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  • PROTEIN
    • Structure
      • Primary
        • Number, type and sequence of amino acids in a polypeptide chain
      • Secondary
        • beta-pleated sheet
          • More rigid and less flexible than the helix
          • e.g. collagen (tendons and skin), myosin (muscles)
          • Typical of structural proteins
        • alpha helix
          • High tensile strength
          • 3.6 amino acid residues per turn of the helix
        • Shape of the polypeptide chain (maintained by hydrogen bonds)
      • Tertiary
        • Precise, globular, compact, 3D shape
        • Maintained by four types of bond
          • Disulphide
            • R groups of Sulphur
          • Ionic
            • Amino and carboxyl groups
          • Hydrophobic
            • Involving amino acids with hydrophobic R groups
          • Hydrogen
            • Many present but weak, easily broken
        • the fold of the polypeptide chain
      • Quaternary
        • Two or more polypeptide chains become bonded together
          • Make up PROTEIN
          • e.g.haemoglobin - has four polypeptide chains
    • Contains the elements Carbon, Hydrogen, Oxygen, Nitrogen (and possibly sulphur)
    • Amino acids
      • Monomers of PROTEIN
        • Shape and properties of protein are decided by the sequence of it's amino acids
      • Two for a dipeptide
      • Three or more form a polypeptide
      • 20 different types
      • Structure
        • Amino/amine group
        • Carboxyl group
        • Hydrogen
        • Variable residue (R-) group
      • Amphoteric: can act as an acid and a base
        • Role as buffer
    • Polypeptide
      • Amino acids joined by Peptide bonds
      • Formed via condensation
      • Broken down via hydrolysis
    • Structure and Function
      • Fibrous
        • Little/no tertiary structure
        • Usually insoluble in water
        • Many structural roles (physically tough)
        • e.g. keratin (hair and nails) and collagen (skin, tendons, ligaments)
      • Globular
        • Complex tertiary and sometimes quaternary structures
        • Spherical globular shape
        • Soluble- hydrophobic side chains
        • Role in metabolic reactions
        • E.g. enzymes, haemoglobin, hormones (insulin) and antibodies
        • Haemoglobin
          • 2 alpha chains and 2 beta chains
          • Nearly spherical
          • Each polypeptide chain has a haem group wihich contains the iron
      • Conjugated
        • Haemoglobin
          • 2 alpha chains and 2 beta chains
          • Nearly spherical
          • Each polypeptide chain has a haem group wihich contains the iron
        • Have a non-protein (prosthetic) group
        • e.g. glycoproteins

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