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  • Proteins
    • Structures
      • Primary Structure
        • The sequence of amino acids.
      • Secondary Structure
        • When H bonding causes a difference in structure- it becomes either a beta pleated sheet or an alpha helix.
      • Tertiary Structure
        • The 3D structure of the protein- when R groups cause ionic bonds, hydrogen bonds, disulfide bridges, and areas that are hydrophilic and hydrophobic.
      • Quaternary Structure
        • The structure and shape caused by multiple polypeptide chains.
    • Fibrous and Globular Proteins
      • Fibrous- collagen
      • Globular- haemoglobin
      • See comparison resource between haemoglobin and collagen.
    • Amino acid monomers
      • Amino acids contain carboxyl group - COOH
      • Also contain an amine group - NH2
      • Also has an R group that differs between the 20 different amino acids, and causes different bonds that make the 3D structure. Can contain sulfur.
    • Two amino acids with a peptide bond = a dipeptide
      • Multiple amino acids with peptide bonds = polypeptide
        • Peptide bonds formed in condensation reactions between hydroxyl group on carboxyl part and H from amine group, so water is released after the bond is formed.
        • Water is used up in hydrolysis reactions when peptide bonds are broken.
    • Protein test with buiret reagent.
      • Turns from blue to lilac.


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