What exactly is this question asking? Part 2

Question

Describe what information concerning the structure of an enzyme could be inferred from your experiment.

I basically did an experiment that proved heat effected enzyme efficiency was influenced by temperature. ie enzymes have optimal performance at a temp range of 40 C to 50 C and that it deteriorates at extremely low or high temps. I know this is caused by the fact that an enzyme is a protein, but what exactly do I say to answer this question? About its structure

Answer 1

All molecules are in motion (except at absolute zero). As the temperature increases, their motion increases too. In the case of enzyme catalyzed reactions, as the speed of enzyme and substrate molecules increases, the chance for collisions so they can form enzyme-substrate complexes increases. Thus as the temperature rises, the reaction rate increases too. Above the optimal temperature however, this does not apply. The reaction rate begins to decrease again because some of the enzyme molecules are now warm enough so that their shape becomes altered (H bonds begin to break, denaturing the enzymes). As the temperature rises above the optimal then, an increasing number of enzymes become denatured (= loss of 3-D structure). Fewer and fewer enzymes are able to fit with their substrates at the active site. The reaction rate decreases until at some high temperature, all the enzymes are denatured, and reactions cease.

Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape.

Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted.