 So I briefly describe the secretion assay that we used to estimate the functions of these mutants. So this is a cartoon of the experimental setup we used to perform the assay. It has, so there is a rotating disk electrode, or IDE, which is made of a classy carbon that is suspended into a sample chamber. And the principle of the assay is based on the electro oxidation of norepinephrine. So when norepinephrine is present in the sample chamber and it contacts the IDE on the rotating disk electrode, it is oxidized. And the change in oxidation potential of the rotated disk electrode can be measured with respect to a reference electrode and can be recorded by an output device. And so we used cracked cells for mutilized cells, which are capable of secreting norepinephrine, and added them to the sample chamber. So what is done to these cells so that they are mechanized, they are homogenized, and their cytosol is removed, but their membranes are preserved intact during the process. And then they are suspended in a physiological buffer, and the test factor, which in this case are caps mutants, are then added to it to test their activity. And this entire cell suspension is put in the sample chamber and then calcium is added to it to trigger exocytosis. And depending on the IDE signal that we get, we would be able to tell whether it increases caps function beyond that of the wild type caps, or whether it reduced caps function, because the amplitude of the signal, which is obtained from the experiment, is proportional to the number of norepinephrine vesicles released. And the good thing about this STA is that it has very high sensitivity, so even small quantities of norepinephrine veins can be detected. So these are our results from the IDE secretion analysis. We find that the 957 to 961 aniline mutant, it has almost the same activity as our wild type, so it is not exactly very interesting. Although this is a surprising finding, because we would expect that because it is within the monchromology domain 1, it would show some activity. And as a second mutant, however, the 1134, 1138 aniline mutant, which lay the seat on the segment of caps protein, it did show some reduction in activity as compared to wild type. So it goes around 75% activity as a wild type. So this graph again shows the comparison better. As in, this is the wild type voltage which is recorded, and this is the voltage recorded using the 1134 to 1138 aniline mutant. So the conclusions from the experiments that we have done are that the conserved residues in monchromology domain may be important for proper folding of caps. That is the reasons why we also update distributions of the protein. Second is that the secretion assay data that we have suggests that 1134 to 1138 aniline mutant shows reduced activity, but we do not know yet what the exact reason for that is. So more experiments need to be performed before we are able to conclude what is exactly the reason. That is, the caps 957 to 61 mutant does not reduce capsicility integration. So it presumably does not lie in the exact snare binding region within the capsic protein. So these are the references that I've used for making the presentation and acknowledgments to the Korana program, Department of Biotechnology in the U.S. Science and Technology Forum in UW-Madison for Funding Bioproject, to Professor Tom Martin for hosting Nina's lab, and to Neil and all members of the Martin lab. They've been extremely helpful and they've offered guidance whenever I've asked for it, and the 2011 Korana fellows and the audience for paying attention.