Hi guys!

Anyway this is a proteins mindmap for OCR F212 exam and it is for biological molecules.

Don't just read this revision, use it.

If you are stuck for this exam, message me.

Good luck!

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  • Proteins
    • Structure
      • There are 20 amino acids and this varies because of the different R groups.
        • You need to know cysteine and glyceine.
      • There is an amine and carboxyl group-you need to be able to identify these.
      • The monomer is an amino acid.
      • Nitrogen, carbon, hydrogen and oxygen are the elements present.
      • It is a condensation and hydrolusis reaction.
    • Primary structure
      • Sequence of amino acids in a polypeptide. They are joined by a PEPTIDE BOND.
      • Determined by the sequence of bases in RNA.
    • Secondary structure
      • Polypeptide chains are rarely straight lines. The way the polypeptide chains coils or folds is the secondary structure.
      • Either alpha helix (coils) and beta pleated sheet (zig zag).
        • They can be both in a protein but it depends on the R group.
      • Hydrogen bonds are important.
        • Helps stabilise it.
    • Tertiary structure
      • The overall 3D shape caused by further folding of the polypeptide.
      • Held together by hydrogen, ionic and hydrophilic / hydrophobic interactions.
      • Responsible for the shape of amino acids.
      • Shape of channel in channel proteins.
      • Denaturing disrupts the tertiary structure; 3D shape changed because of the breaking hydrogen, ionic and hydrophilic/hydrophobic interactions.
    • Quaternary structure
      • This  includes more than one polypeptide.
      • Haemoglobin
        • Alpha and beta subunits.
        • Prosthetic groups (haem)
        • *No disulphide bonds to stabilise the structure*
        • Globular
          • Ball shaped molecules.
          • Metabolic roles
      • Collagen
        • Fibrous
          • Long strands
          • Structural roles
          • Insoluble
        • Ends are staggered so they are no weak points.


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