| March 14, 2016

1) A very brief background of the protein. Why is the protein important? What pathway does it participate in?
2) A brief description of the purification of the protein. Was it overexpressed or isolated from a native source? Often, people refer to prior papers for these descriptions so you may have to consult a reference here.
3) What type of assay was used? Was it continuous or fixed time? Was it spectrophotometric, radioactive, coupled, etc. Sometimes the assay is referenced also.
4) The kinetic and/or binding constants for at least one substrate or ligand. What do these constants mean? Why do the constants matter (Ex: since the binding of the inhibitor to the enzyme is very tight, it may be clinically effective)?
5) Were other experiments done such as assays of mutant proteins or assays of other substrates? What do the relative kinetic constants indicate (Ex: a mutation converting a serine to an alanine rendered the enzyme inactive but still able to bind the substrate indicating that the serine is likely to be catalytic).

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