Exploring the Capacity of Proteins to Switch their Three-Dimensional Structures and Gain New Function
Proteins are the machinery of the cell that carryout the processes necessary to sustain life. The unique 3-dimensional structures of proteins are crucial for their specific functions in the cell. The goal of my research is to understand the fundamental properties of protein structure and determine experimentally the mutations in protein sequence that can trigger large-scale changes in its 3-dimensional structure. To accomplish this, I am investigating the mechanisms by which two proteins with high sequence identity but different 3-dimensional structures and functions can flip from one structural state to another. I use a directed evolution technique to screen all the possible mutations in the non-identity regions of the protein sequence that can trigger a structural switch from one 3-dimensional state to another, which is accompanied with a new function.
My research addresses a fundamental question of how protein sequence codes for the 3-dimensional structure of protein. This research also provides a framework for understanding the evolution of new functional proteins from existing ones. Results from this project will have relevance to developing improved computational protein structure prediction programs, understanding the evolution of protein structures, enhancing protein engineering approaches, and interpreting mutations in some human diseases.
Tsega Solomon is currently a doctoral candidate in the Department of Chemistry and Biochemistry at the University of Maryland. She has a Bachelor of Science in Chemistry from the University of Virginia. Tsega was awarded the Dolphus E. Milligan Graduate Fellowship by the National Institute of Standard and Technology and the University of Maryland.