Hellloooo, going to try my best to answer your questions hahah
What is the site on an enzyme that a non-competitive inhibitor binds to?
any site other than the active site
Also, some enzymes are not primarily composed of proteins, right? For example, an enzyme could be inactive until a cofactor binds to it, so the enzyme is essentially composed of a protein part, and a non-organic non-protein part. So could you call the protein part the enzyme, or is the 'whole' structure (by this I mean including the cofactor) called the enzyme?
apoenzyme = protein portion. you probably don't need to know this but apoenzyme + coenzyme = holoenzyme
Oh and when a non-competitive inhibitor binds to the enzyme, it will deform the shape of the enzyme and consequently break the R-group/variable interractions. What is the proper term instead of 'break' the interractions?
I'm not sure, but I think you only need to know that it changes the active site.
Last question, promise. When the temperature is decreased in an enzyme-catalysed reaction, does it reduce the molecular kinetic movement of the substrate and enzyme, henceforth reducing the opportunity for the subtrate to bind to the cleft of the enzyme? If so, what about enzyme's whose optimum temperature is really low, does this mean that the molecular movements are still slow, but does this mean that the enzymatic activity is generally slow or is this beyond the scope of VCE biology?
yes, hmm i don't know an enzyme which has a very low optimum temperature... but ALL molecules move slower at lower temperatures
Also, when an enzyme is exposed to it's optimum conditions/environments, does it perform at it's optimal ability? Is that the correct term?
I believe so.
you sound a little stressed, i don't think you need to worry about such technicalities and terms