Effects of Chaperonin on protein folding

The effects of chaperonin on protein folding were determined in the experiment and supported the hypothesis that the chaperonin protein, when its sequence was inhibited, results in mutated E. coli cells. Following the procedure, the experimenter altered the chaperonin DNA sequence of E. coli, inserted it into the cells, plated the experimental and control samples, and incubated them. After six days, a color change in the experimental E. coli cells, visible to the naked eye, was observed. Upon further investigation of the growth under a microscope on 40x magnification, it was determined that the experimental E. coli cells that were yellow in color appeared morphologically different from the white experimental and control cells. The typical white cells had a bacillus structure, where the yellow cells had smaller, coccus structures. The size of a single cell was averaged from each microscope image using ImageJ software. The results were compared and it was concluded that the size of the yellow experimental E. coli were affected by the alteration of the chaperonin DNA coding sequence that was inserted into the experimental E. coli sample. The chaperonin protein is a key contributor to preventing misfolded proteins from creating mutations in living organisms. Knowing the effects of chaperonin being inhibited in an organism can help scientists better understand its function and importance in cells and in organisms as a whole.