Please enable JavaScript.

Coggle requires JavaScript to display documents.

Biology Chapter 1-5 - Coggle Diagram

- - - - Primary:
        
        Sequence of amino acids bonded by covalent peptide bonds is the primary structure.
        
        DNA of a cell determines the primary structure by instructing the cell to add certain amino acids in specific quantities in a certain sequence. Affects shape and function.
        
        Specific for each protein.
      - Secondary:
        
        Occurs when the weak negatively charged nitrogen and oxygen atoms interact with the weak positively charged hydrogen atoms to form hydrogen bonds. a- helix and B-pleated sheet.
        
        a-helix shape occurs when the hydrogen bonds form between every fourth peptide bond.
        
        B-pleated sheet shape forms when the protein folds so that two parts of the polypeptide chain are parallel to each other.
        
        Fibrous proteins have secondary structure.
      - Tertiary:
        
        Additional bonds forming between R groups.
        
        Hydrogen, disulphide, ionic and weak hydrophobic interactions.
        
        Structure common in globular proteins.
      - Quaternary:
        
        Occurs in proteins that have more than one polypeptide chain working together as a functional macromolecule, haemoglobin.
        
        Each polypeptide chain is referred to as a subunit of the protein.
- - - - Converting units of measurement:
        
        There are 1000 nanometers (nm) in a micrometer.
        
        There are 1000 micrometers in a millimetre (mm).
        
        There are 1000 millimetres (mm) in a metre (m).
- - - - Channel proteins:
        
        Water-filled pores.
        
        Allow charged substances to diffuse through the cell membrane.
        
        Diffusion of these ions does not occur freely, most channel proteins are 'gated' meaning that part of the channel protein on the inside surface of the membrane can move in order to close or open the pore.
        
        Allows channel protein to control the exchange of ions.
      - Carrier proteins:
        
        Can switch between two shapes. Causes the binding site of the carrier proteins to be open on one side of the membrane first, and then open the other side of the membrane when the carrier protein switches shape.
        
        Direction of movement of molecules diffusing across the membrane depends on their relative concentration on each side of the membrane.