As a man whose skills are related to bioinformatics, protein expression, biochemistry, and “general troublemaking,” Dr. Paul Smith has a lot on his hands. Dr. Paul Smith is currently a professor in the Chemistry Department at Fordham’s Rose Hill campus who divvies up his time between teaching and carrying out multiple laboratory research projects. Smith is a graduate of Columbia University where he received his Doctor of Philosophy in Molecular Biophysics and Biophysical Chemistry in 2005.

Smith had not been involved in research until his senior year of undergrad where he took a project laboratory class at Columbia University, allowing him and several other students to conduct research projects in exchange for credits. The professor of this class cultivated Smith’s interest in research, leading Smith to attend graduate school. While completing post-doctoral work at Memorial Sloan Kettering, Smith conducted research in the molecular biology department. After his time at Sloan Kettering, Smith became a teacher and researcher at Fordham University in 2013.

Smith is currently conducting research in two different branches, one computational and the other on structure-function relationships for proteins. Under the structure-function branch of research, Smith is studying the relationship between atoms and how this relationship may impart function, whether it be enzymatic, structural or more. Under this course of study, Smith was approached by associates at Weill Cornell Medical College to conduct research on E4ORF1, a protein with unique attributes to it that have “potential in biotechnology applications.”

E4ORF1 is a viral protein, which is associated with adenoviruses, that radically alters cell physiology. Smith states that adenoviruses are pathogens implicated in sickness and disease, such as the common cold, obesity, and diabetes. These proteins have unique abilities to affect other cells and proteins. In his proposal, Smith suggests, “One of these genes in particular, orf1, has been shown to have remarkable ability to alter cellular physiology upon expression.” E4ORF1 is an aggregation-prone protein that forms a precipitate in solution that is difficult to dissolve, even with the strongest of agents.

The goal of his research is to identify the structure of this protein and its aggregation abilities in relationship to other proteins and cells. Although the protein is small, its structure is unknown. Using computer modelling, Smith has been able to predict the unique hook shape of the protein that may allow it to form fibers. Future applications regarding this protein may be in the growth of hematopoietic cells, which are stem cells that give rise to blood. With further research work, there may be the ability to grow these cells without growth factors by simply using this protein in culture. This would reduce the risk of rejection in transplants and transfusions.

Smith compares research work to wildcatting, which is exploratory oil well drilling. In discussing his analogy during our interview, Smith states “You sink a drill and you hope you get lucky… you might make it rich or you might end up broke.” Protein work is unpredictable and crystallization or finding a protein with unique biochemical traits that can be traced is difficult. Nevertheless, Smith has a great outlook for the future of his collaborative research project and hopes that purification and application of the E4ORF1 protein will be possible in the near future.