And, Another Copout

Below is the final abstract for my paper (same name), and I can say that I am completely relieved to be done with its 27 pages. To be fair, it would be closer to 25 pages in terms of actual content; as in, there are some large blank spaces that had to unfortunately exist due to graphs and tables being too large. 

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Two distinct mutants of HPII catalase were made by incorporating Aminophenylalanine and O-methyl-L tyrosine respectively at site 392, thus creating novel interactions, to investigate the structure and activity of HPII catalase. The oxygen generation rate was measured as a function of initial hydrogen peroxide concentration for wildtype catalase and translated into catalytic constants using Michaelis-Menten kinetics. The catalytic constant  was 6.25 s^-1 whereas the Michaelis-Menten constant  was 330 mM, which is inconsistent with literature values (  and   = 100800 s^-1).  The O-methyl-L-tyrosine (  =  s^-1 and ) and Aminophenylalanine mutants (  =  s^-1 and  feature substantially lower activity and affinity for hydrogen peroxide than wildtype catalase, which is consistent with previous site-directed mutagenesis studies on this site.

In particular, the increased steric hindrance, which can be approximated using molecular size, presented by both UAAs likely resulted in the knockdown of catalytic activity by preventing the His392-Tyr415 linkage from forming. Performing a subsequent denaturation assay with 3.6 M Guanidine Chloride differentiated the AF mutant and the OMT mutant, which have a similar molecular size, on the basis of activity, suggesting that steric hindrance in conjunction with the presence of reactive side groups such as AF’s nitro group drives activity.

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 On that note, I intend to edit and upload a blog post I wrote a few days ago. I hope to actually get to writing another blog post. Wednesday at 8 pm is that magical time that I will be free to do as I wish. So, blogs!