kinetics

Hi SDN! I was wondering what the relationship between cooperativity and entropy is with regards to hemoglobin and oxygen binding. I came across a question in TPR biochem review on this topic and in the answer description it says "consistent with the 'cooperativity' phenomenon of each of these...

As a general question in kinetics, when we are under LOW conditions of substrate, do we want HIGH or LOW affinity for the substrate? I have in my notes that when we are under low substrate conditions, we want low affinity for the substrate because we don't want to be using it up so much since...

Can someone please explain how to find this answer to me? Researchers collected the following data for an enzyme-catalyzed reaction. [Substrate] (muM) 3 6 10 20 50 100 1000 10,000 Vo (muM/min) 22 53 100 129 162 180 199 200 What is the approximate numerical value of the slope of the...

The reaction 2A + B <--> C + D is found to take place in two steps, the first, which follows second order kinetics is slow and the second is fast. Which of the following CANNOT be the mechanism for the rate determining step of this reaction? A) A collides with B B) A collides with A C) B...

The only irreversible competitive chemicals/drugs that comes to my mind are Aspirin, phenoxybenzamine, and (maybe CO toxin? or that one maybe just has a REALLY high affinity and may be CONSIDERED irreversible). Does anyone have a compilation of these irreversible competitive inhibitors? feel...

Competitive inhibitors don't change Vmax, while uncompetitive/noncompetitive inhibitors do. Why? They all do the same basic thing - prevent substrate from being processed by the enzyme. But the way they do it is different. However, for the purposes of my question, please address the following...