PHD Biochemistry Sample Personal Purpose Statement

PHD Biochemistry Sample Personal Purpose Statement Help

I am enthusiastic about joining your program because I believe my greatest contribution to society would be to help discover new disease treatment methods, based on a deeper understanding of disease origins and propagation mechanisms. I am a committed student, determined to achieve professional success, partly due to overcoming numerous challenges to reach my current position. As an Algerian American woman born in the USA and raised in Algeria until age thirteen, I faced many first-generation immigrant challenges, adapting to a new culture, language, and educational system.

For many years, I have aspired to excel as a scientist, particularly in the study of diseases. This ambition led me to pursue physical sciences as an undergraduate and complete my master's in Biochemistry. My research interests focus on protein interaction and neuro-degenerative diseases. I aim for a long, productive career as a research scientist in academia. My strong candidacy for your program is not only due to my rigorous academic preparation but also my professional and volunteer experiences. I gained valuable insights working as a research associate for five years after earning my BS degree and volunteering at an open-heart surgery hospital, which deepened my understanding of heart disease causes across ages. I am highly motivated, characterized by perseverance and curiosity, and I thrive on challenges.

My fascination with scientific research methods grew over time. During my undergraduate studies, my family faced severe hardships that negatively impacted my grades; however, I persevered and my grades significantly improved as I delved into the study of atomic structures, bodily processes, functions, and major biochemical discoveries. I particularly enjoyed my courses in organic chemistry, biochemistry, and laboratory work.

I have both managed my research projects and collaborated on those of colleagues in other labs. Discovering new paths for drug discovery through diverse experimental approaches was exhilarating and rewarding. Working alongside PhD students spurred my growth as a scientist and convinced me to pursue a PhD. I am a results-oriented investigator eager to enhance my expertise through doctoral studies at your esteemed research university. I am particularly interested in researching ligand/substrate interactions and their effects on human systems, from cell signaling to protein synthesis, with a focus on neurodegenerative diseases. I have a history of collaborating with senior researchers and a track record of completing research within project parameters. I am skilled in using laboratory instruments, equipment, and software for complex data collection and analysis. I am detail-oriented, especially regarding data validity, accuracy, and outcomes.

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 four years. I particularly enjoyed studying the regulation of intramembrane proteolysis (IMP). The potential link between the proteolysis of the dimeric form of the Amyloid precursor protein (APP) within the transmembrane domain by g-secretase and the accumulation of toxic b-amyloid in the synaptic compartment, leading to Alzheimer’s disease, excites me. I conducted kinetic studies using fluorescent resonance energy transfer (FRET) to assess APP dimerization and developed a FRET-based assay to identify small molecular determinants necessary for APP-b CTF dimerization. The FRET assay proved sensitive for monitoring b CTF dimerization and dissociation. I designed small chimeric peptide inhibitors assumed to inhibit dimerization by binding to dimer interface motifs. Additionally, I performed large-scale screening of small molecular chemical compounds with drug-like properties, adhering to most of Lipinski’s rules, to inhibit dimerization.

Moreover, I worked on another study focused on the regulation of intramembrane proteolysis (IMP) proteins and Rhomboids involved in the epidermal growth factor receptor ligands Spitz, Gurkeen, and Keren. The study aimed to answer two key questions: how do IMPs recognize their substrates, and how is the scissile peptide bond selected? Our goal was to determine the rhomboid's substrate specificity. I constructed chimeric substrates with transmembrane domains and used mass spectrometry to analyze proteolytic products, verify enzyme activity, and determine cleavage site specificity. By mutating thirty amino acid residues of the transmembrane domain, I identified mutation effects and analyzed cleavage site importance. I discovered that the enzyme is sequence-specific and, when mutated, the cleavage site shifts to the nearest similar amino acid residue recognized by the enzyme.

I have a proven track record of supporting and contributing to high-quality scientific research. I am eager to bring my expertise and experience to your program, confident in my potential to excel.

PHD Biochemistry Sample Personal Purpose Statement Help