Describe the structural properties of a globular protein.

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What is meant by an active site? What determines the specific shape of an enzyme's active site? What does the shape of the substrate need to be in relation to the active site of an enzyme? What does a reduction in activation energy mean? What is activation energy? How does the formation of an enzyme-substrate complex lower the activation energy? What is the lock and key model? Why might the lock and key model be incorrect? What is the induced fit model? How does the induced fit model explain the specificity of enzymes? How does temperature influence enzyme activity? What happens if temperature of an enzymatic reaction gets too high? What is meant by an enzyme being denatured? What is meant by the optimum temperature? What is the optimum temperature of most human enzymes? What is the temperature coefficient? How can the temperature coefficient be measured? What is the rough Q10 value of most enzyme-controlled reactions? What is meant by an optimum pH value? 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Is a vitamin a cofactor or a coenzyme? What do cofactors do? What is a tightly bound cofactor known as? What is the prosthetic group for carbonic anhydrase? What is the role of enzyme inhibitors? What is competitive inhibition? What shape do competitive inhibitors have? During competitive inhibition, what impacts how much the enzyme is inhibited? What does increasing the concentration of substrate do during competitive inhibition? What is non-competitive inhibition? What does a non-competitive inhibitor do to the active site of an enzyme? What effect on rate of reaction does an increase in substrate concentration do during non-competitive inhibition? What is the allosteric site? What is the difference between reversible and non-reversible inhibitors? What sort of bonds are involved in irreversible enzyme inhibition? What sort of bonds will be involved in reversible enzyme inhibition? Give examples of medicinal drugs as enzyme inhibitors. 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