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l ask to be admitted to your program because I am convinced that the greatest contribution that I might be able to make to society would be to contribute to the search for new avenues for disease treatment based on an improved understanding of the origins of disease and its propagation. I am a very serious student and highly determined to succeed professionally, in part, because I have already overcome so many obstacles to get to where I am at this point in my life. I am an Algerian-American woman who, while born in the USA, was raised in Algeria until the age of 13. As a result, I have had to overcome many of the difficulties of the first-generation immigrant having to adjust to a foreign culture and a different language as well as a new educational system.
I have known for many years that I wanted to succeed as a scientist and that it would be in the study of disease where I wanted to make my mark on life. This is why I studied the physical sciences as an undergraduate student and have now completed my Master’s Degree in Biochemistry. I am especially interested in doing research in the areas of protein interaction and the study of neuro-degenerative diseases. I look forward to a long and productive career as a research scientist in an academic setting. I feel strongly that I am a strong candidate for your program not only as a result of my intensive academic preparation but also y professional and volunteer experience. I learned a great deal by working as a research associate for 5 years following the completion of my BS degree. In addition to volunteering in an open heart surgery hospital, enhancing my understanding of the causes of heart disease among old and young people alike. I am a highly motivated individual characterized by both my perseverance and my inquisitiveness and I thrive on challenges.
As I was growing up, I became increasingly fascinated by the methods used for scientific research and discovery. My family and I experienced some extremely difficult circumstances while was an undergraduate student that had a most negative impact on my grades; nevertheless, I did not give up. Instead, I bounced back and my grades soon started to radically improve. As a student, I became complete immersed in the study of the atomic world of bodily processes and functions, especially the great biochemical discoveries of modern times. As an undergraduate student, I immensely enjoyed my courses in organic chemistry and biochemistry, and especially my laboratory courses.
I have managed my own research projects as well as collaborating with those of colleagues in other labs. I found it to be the most exhilarating and rewarding experience to work hard in finding new avenues for drug discovery using a broad variety of experimental approaches. I generally worked alongside PhD students which helped to spur my own maturation as a scientist and convincing me that I too should undertake study towards the PHD. I am a results-oriented investigator who is eager to further enhance my expertise by studying towards the doctoral degree at your leading research university. I am especially keen to do research in the area of ligand/substrates interactions and their effects on all human systems from cell signaling to protein synthesis, especially with respect to developing a better understanding of neurodegenerative diseases. I have a history of collaboration with senior researchers and a proven track record of accomplishing assigned research within project parameters. I am highly adept at the use of laboratory instruments, equipment, and software programs for the collection and analysis of complex data. I am highly focused and quality-oriented with attention to detail, especially data validity, accuracy, and outcome.
I have worked at both the XXXX School of Medicine in the Structural Biology Department and as an Associate Researcher for the XXX College of New York for the past 4 years. I have especially enjoyed working on a study of the regulation of intramembrane proteolysis (IMP). I am especially excited by the fact that the Proteolysis of the dimeric form of the Amyloid precursor protein (APP) within the transmembrane domain by g- secretase, could lead to the accumulation of toxic b -amyloid in the synaptic compartment resulting in Alzheimer’s disease. I have carried out kinetic studies using Flourecent resonance energy transfer (FRET) to assess the dimerization amyloid precursor protein and developed a FRET based assay in order to find small molecular determinants required for the dimerization of APP- b CTF. The FRET assay was proved to be very sensitive when monitoring the b CTF dimerization and dissociation. I designed small chimeric peptides inhibitors that were assumed to inhibit the dimerization by binding to the dimer interface motifs. I also have preformed large-scale screening of small molecular chemical compounds possessing drug like properties satisfying most of Lipinski’s rule, to inhibit dimerization.
Finally, I have worked on another study concerned with the regulation of intramembrane proteolysis (IMP) proteins and the Rhomboids involved in the epidermal growth factor of receptor ligands Spitz, Gurken and keren. The aim was to answer two key questions: first, how do IMPs recognize their substrates? Second, how is the scissible peptide bond selected. Our goal was to find the specificity of the rhomboid to its substrate. I constructed Chimeric substrates containing the transmembrane domains and then used mass spectrometry for the analysis of the proteolytic products to verify the activity of the enzyme and determine the cleavage site specificity of this enzyme. I mutated the 30 amino acid residues of the transmembrane domain in order to identify the effects of the mutation and analyze the importance of the cleavage site. I was able to determine that the enzyme is sequence specific and, when mutated, the cleavage site moves to the nearest similar amino acid residue recognized by the enzyme.
I possess a proven track record of supporting and contributing to high-caliber scientific research. I am eager to bring my expertise and experience to your program where I am convinced that I have the potential to excel.