Structure of the enzyme using only the sequence of amino acids
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Secondary
Structure of the enzyme as a result of coiling/folding due to the presence of hydrogen bonds. The protein chain can fold into an alpha helix or a beta pleated sheet
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Tertiary
Structure of the enzyme as an overall 3D shape of a protein molecule. It is the result of interactions between groups of the protein molecule, e.g. ionic, hydrogen bonding, disulfide bridges, hydrophobic/hydrophilic interactions
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Quarternary
Structure of the enzyme where a protein consists of more than one polypeptide chain, e.g. haemoglobin. They are held together by the same types of forces shown by tertiary enzymes
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Lock and key
A model where the R groups of the substrate must perfectly complement the R groups of the polypeptide chain in the enzyme in order to bind, i.e. charge and shape
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Catalyst
This provides an alternate route for a reaction to take place with a lower activation energy. It has a transition state (highest energy state)
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Induced fit
A model where the enzyme binds to the substrate and slightly changes its structure to better fit. This stabilises the transition state, reducing the energy required.
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Vmax
The maximum rate of reaction an enzyme can support (at saturating substrate) when the substrate is no longer the limiting factor and the rate of reaction is the highest it can be
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Km
The substrate concentration when the reaction velocity is half of Vmax. It measures how quickly a reaction rate increases with substrate concentration. A low Km corresponds to a higher affinity for the substrate
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Competitive
Inhibitors that compete with substrates for active sites on the enzyme, so that less substrate can bind. Same Vmax, increased Km
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Non-competitive
This inhibitor and substrate don't affect one another's binding to the enzyme. But when the inhibitor is bound, the enzyme cannot catalyse its reaction to produce the product. Lower Vmax, same Km
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Other cards in this set
Card 2
Front
Structure of the enzyme as a result of coiling/folding due to the presence of hydrogen bonds. The protein chain can fold into an alpha helix or a beta pleated sheet
Back
Secondary
Card 3
Front
Structure of the enzyme as an overall 3D shape of a protein molecule. It is the result of interactions between groups of the protein molecule, e.g. ionic, hydrogen bonding, disulfide bridges, hydrophobic/hydrophilic interactions
Back
Card 4
Front
Structure of the enzyme where a protein consists of more than one polypeptide chain, e.g. haemoglobin. They are held together by the same types of forces shown by tertiary enzymes
Back
Card 5
Front
A model where the R groups of the substrate must perfectly complement the R groups of the polypeptide chain in the enzyme in order to bind, i.e. charge and shape
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