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Proteins B1.2 - Coggle Diagram

- - - - Carboxyl Group
      - Amino Group
      - R-Group
        
        Determines Chemical and Physical Properties of the Amino Acid
        
        Can be Polar
        
        Non-Polar
        
        Hydrophobic
        
        Hydrophilic
        
        Acidic
        
        Basic
        
        Linear
        
        Or Ringed
      - Hydrogen Atom
  - - - Hydrophobic R-groups are non-polar and repel water
      - Hydrophilic R-groups are polar or charged and attrct water
      - R-groups can gain or lose hydrogen ions, resulting in a positively or negatively charged R-group
      - Cysteine R-groups form disulfide covalent bonds which are strong and essential for stability
- - - - H2O released = OH lost from carboxyl + H lost from amino group
      - This forms a Peptide Bond (CO-NH)
      - Examples
        
        Water + Dipeptide = Amino Acid + Amino Acid
        
        Polypeptide = many Amino Acids joined together
    - - N-terminal: amino group end
      - C-terminal: carboxyl group end
  - - - Transcription (DNA to mRNA)
      - Translation (mRNA to ribosome)
      - Codons (3 bases adjacent to eachother, coding for an Amino Acid)
- - - - The sequence of amino acids
    - - Local folding patterns of a polypeptide
        
        Alpha Helices: H-bond between amine H and carboxyl O, four residues apart
        
        Beta-pleated sheets: Parallel, regular H-bonds between the residues of a strand
    - - The overall 3-dimensional shape of a polypeptide, caused by the interactions between R-groups
        
        Protein structure = protein function
        
        Denaturation caused by pH or temperature will cause the protein to lose its structure, therefore function
        
        Hydrophobic interactions lead to a protein with a hydrophobic interior and a hydrophilic exterior
        
        Integral Proteins
        
        Globular Proteins such as Insulin, Haemoglobin, and Myoglobin
    - - The arrangement of multiple polypeptides chains
        
        Protein Folding (the process of a protein adopting a 3-dimensional shape)
        
        Globular Proteins
        
        Compact, Spherical, and Water-soluble
        
        Functions: Enzymes, Transporters, and Regulators
        
        Examples: Insulin, Haemoglobin, and Myoglobin
        
        Fibrous Proteins
        
        Long, Narrow, Repetitive, and Insoluble
        
        Structural Support
        
        Example: Collagen has a triple helix of three polypeptides, with stabilizing hydrogen bonds and van de Waals forces
        
        Types of Polypeptide Subunits
        
        Alpha-chain
        
        Beta-chain
        
        Haemoglobin is made up of 2 a-chains and 2 b-chains with conformational change due to oxygen binding