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About Me: I am interested in developing chemical techniques that give us a deeper understanding of biology. To do this, I would like to continue developing selective chemical probes to perturb and study biological systems. I plan to pursue a PhD in chemistry or chemical biology to further my understanding of chemical methods development and protein chemistry.
Research Project: Phosphorylation is a post-translational modification to proteins that has roles in signaling and regulation. Phosphorylation is both transient and non-stoichiometric, which means phosphorylated proteins can be in relatively low abundance in the cell. This low abundance, coupled with the fact that phosphorylation makes proteins more difficult to study with mass spectrometry, means that new methods are necessary to understand serine/threonine phosphorylation on a proteome-wide scale. My project aims to selectively modify proteins containing phosphate with chemical handles that can be used to separate these proteins from other cellular proteins. This will enable enrichment of phosphorylated proteins and allow more comprehensive, proteomic mass spectrometry studies . With this tool in hand, phosphorylation events corresponding to disease states will be uncovered which will reveal potential drug targets.
About Me: I am fascinated by the rapidly evolving techniques being implemented in molecular biology research. Currently, I study DNA fragility in the Freudenreich Lab and my desire to perform future research has only increased since I started. My research has also brought me closer to my long-term scientific interest of studying oncology. I plan on applying to DNA repair labs when I apply for a PhD. As for my long-term career goals, I would like to move from performing bench research to clinical research after I get a PhD.
Research Project: My project seeks to evaluate the role of (AT)-repeat length in Common Fragile Site (CFS) breakage, as well as to understand how structure-specific nucleases affect fragility. Common Fragile Sites are large regions of DNA that form gaps on chromosomes under replication stress. A large portion of cancer-related chromosomal deletions have been linked to breakage at Common Fragile Sites. The information provided by our study will be the first analysis of the molecular basis of CFS fragility at the DNA sequence level, and the first description of how nucleases protect from or contribute to fragility at this biologically significant sequence. The nucleases’ identified roles and timing of action could help in understanding how to treat diseases such as cancer, Bloom’s syndrome and Fanconi Anemia.
About Me: I have always been interested in studying the environment, especially in ways that will protect it and remediate the damage caused by humans. I plan to use the skills and experience I am building in chemistry to study the environment in a different way than it is often presented in class. I want to focus on what is happening at the molecular level to understand how ecosystems operate on the organismal level, rather than observing changes in the environment and inferring the causes. I am currently conducting research in analytical chemistry, and hope to continue chemistry research through graduate school and beyond to ultimately become an expert in environmental chemistry.
Research Project: In Iceland are approximately 100-meter deep lakes present underneath glaciers atop active volcanoes. Bacteria have been found to exist in these isolated environments with little to no exposure to oxygen or sunlight. The goal of this project is to find the detailed chemical composition of the lake to understand the energy cycles of these unusual organisms. The project will consist of building an array of sensors to conduct measurements in the environment, rather than from extracted samples to preserve the chemistry of the solution, as the sample can change when it is removed from the lake and sent to a lab. Challenges of this project include calibrating the sensors to work under high pressures and finding a reliable way to sense sulfur species, compounds especially of importance in chemosynthetic metabolisms. The chemical will describe the type of environment these organisms live in and what energy sources are present. Since this ecosystem is isolated from sunlight and from oxygen, it may be a good model for the environment of early Earth and of extraterrestrial environments.
Majors: ACS Chemistry, Biotechnology
Graduation: Spring 2016
About Me: I am interested in elucidating the chemical principles essential to understanding the structure and function of biological molecules with computational modeling and simulation. I plan to continue research in computational chemistry while working towards a Ph.D. and ultimately aspire to conduct research at the interface of chemistry and biology with the potential to impact the ways we utilize biotechnology and treat disease.
Research Project: Glycosylation is a common covalent modification on more than half of all proteins. Glycosylation occurs in many different combinations of sugars and linkages, greatly enhancing the diversity of protein chemistries, structures, and functions. In general, glycoproteins must be properly glycosylated to achieve their full bioactivity; altered glycosylation is linked to the pathophysiology of diseases ranging from cancer to rheumatoid arthritis. Currently, the impact of glycosylation on protein structure is poorly understood and difficult to predict. Although specific protein-sugar interactions are believed to contribute to structural stability, very few universal interaction patterns have been identified. I am utilizing structural bioinformatics to discern protein-sugar interactions that contribute to structural stability. Molecular dynamics simulations will be utilized to quantify the protein-sugar energetics. Molecular level knowledge of how sugars mediate protein structure will further our understanding of the intrinsic biophysical properties of glycoproteins and will enable glycosylation to be used to engineer novel protein structures and functions.
Graduation: Spring 2016
About Me: Although I have always been fascinated by living things, my desire to pursue research as a career has been cemented during my time at Tufts. Embarking on an independent research project in the fields of developmental and regenerative biology has shown me how exciting and deeply fulfilling scientific discovery can be. In the future, I hope to earn a Ph.D. in biology, and then begin a career in biological research.
Research Project: My project has focused on exploring information storage in biological systems, involving an integration of genotype, phenotype, environment, and developmental history. Specifically, I am interested in complex phenotypes, like head shape or resilience to an environmental insult, in the planarian flatworm. The influence of bioelectricity on the anterior/posterior patterning of the planarian has been thoroughly characterized, but my project represents the first time bioelectricity has been implicated in the production of shape. I am also investigating the robustness of bioelectric homeostases after exposure to environmental insult, like an ion channel blocker. Overall, my project is unique in its approach to high-level questions about biological information storage and organization. Exploring complex systems like regeneration, development, and oncogenesis with attention to epigenetic, environmental, bioelectric, and physiological sources of information will add to medicine, engineering, and an overall understanding of the complexity of life.
Majors: Biochemistry and English
Graduation: Spring 2015
About Me: My desire to explore science beyond the concepts and methods one learns in class, led me to pursue research. I wanted to use what I was learning in my chemistry and biology courses to investigate the factors affecting human health and disease on a molecular and cellular level.
Research Project: My desire to use chemistry to attack biological problems is reflected in my project, designing cyclic peptide inhibitors of the EH domains of Reps1 and Eps15. These proteins are involved in endocytotic and vesicle trafficking pathways in the cell, and coordinate these processes with epidermal growth factor receptor (EGFR) signaling. The proposed peptides will inhibit specific protein-protein interactions between Reps1 and Eps15 and their binding partners, providing new tools for studying the roles of these proteins in normal cell processes and in tumor development.
John Lawrence III
Major: ACS-Certified Chemistry
Graduation: Spring 2014
About Me: My current scientific interest lies in photochemistry and polymer chemistry. More specifically, I have become attracted to the growing field of organic electronics. Electronics have become extremely prevalent in today’s society, and introducing organic chemistry into the production of electronics would alleviate some of the burden that the current materials used put on our environment. As a self-proclaimed “green” chemist, I am conscious of our effect on our planet. I would like to minimize the negative repercussions that the current production methods have environmentally by creating organic alternatives.
Research Project: My project aims to create photo-reactive polyelectrolyte multilayer films (PEMs) comprising charged polythiophene (PT) manufactured using layer-by-layer (LbL) assembly. By using polythiophene, we hope to produce semiconducting polymer films that are applicable to photolithography, the fabrication of printed circuit boards, and microelectronics. Our ideal application of the product would be the construction of photopatternable electronic materials.
Graduation: Spring 2014
About Me: I aspire to be a physician-scientist. My short term goal as a Beckman Fellow is to contribute to the research efforts of the Freudenreich Lab in the hope of making discoveries that will ultimately impact Huntington’s disease and Amyotrophic Lateral Sclerosis (ALS) patients. My long term goals include plans to apply to MD/PhD programs to launch my career in biomedical research.
Research Project: Expansion of DNA repeats cause a number of neurodegenerative diseases, such as Huntington’s disease, myotonic dystrophy, and most recently a newly discovered DNA repeat that is associated with 20-50% of Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD) cases. The Freudenreich lab has developed a model system to study how these repeats expand and cause chromosome fragility using a yeast artificial chromosome that contains the human repeat expansion. My project will be to incorporate the ALS-causing repeat into this system, and optimize the assay for screens designed to identify genes and factors that influence repeat stability. This work will ultimately shed light on factors and pathways that influence the stability and fragility of the DNA repeats that cause Huntington’s disease and ALS.