I started my research career at Tsinghua University in Dr. Yongbin Yan's and Dr. Haimeng Zhou’s research group as a master student. During my masters degree I used FT-infrared and other spectroscopic methods to study protein unfolding and aggregation of RNAse A. In 2006 I joined the PhD program at the University of North Carolina (Chapel Hill) in the Department of Biochemistry and Biophysics. My work focused on protein dynamics probed by NMR relaxation, under supervision of Dr. Andrew Lee.
I obtained my PhD in 2011 and began my postdoctoral training in Dr. Traci Hall’s group at National Institute of Environmental Health Sciences. My research focused on structural and functional studies of RNA-binding proteins. This postdoc training not only extended my training to crystallography and RNA biology, but also gave me an opportunity to make use of my expertise in NMR dynamics (acquired during my PhD studies). I joined the UAB Chemistry Department as an Assistant Professor in 2016.
My lab will build on research projects developed during my postdoctoral training, focusing on the structure and function of intrinsically disordered proteins. Furthermore, the integration of crystallography, NMR, and other spectroscopic methods greatly widens my research scope and enables me characterize both protein structure and dynamics.
Over 30 percent of the human genome encodes intrinsically disordered protein regions. These disordered regions can co-occur with neighboring folded domains or make up intrinsically disordered proteins alone. Despite being unstructured, intrinsically disordered regions are essential for cell survival and exert regulatory functions by encoding phosphorylation sites. However, the full impact of these regulatory mechanisms on cellular function is still largely unknown. This gap in knowledge is, in part, due to the dynamic nature of these disordered regions that make them difficult to study. Furthermore, dramatic conformational changes, as exemplified frequently by binding-induced protein folding, may also hinder studies seeking to understand the regulatory mechanisms associated with these post-translational modifications.
My lab seeks to understand the regulation of cellular processes through phosphorylation of intrinsically disordered regions of proteins. Because disordered regions regulated by phosphorylation are abundant in RNA-binding, my lab focuses on two excellent examples in histone mRNA stem-loop binding protein and Serine/Arginine rich splicing factors. Phosphorylation plays vital roles in both of these systems. The goal of our research is to understand how phosphorylation of disordered regions found in these proteins provides functional regulation of this class of proteins at the structural level. In addition, we also seek to determine how defects in phosphorylation of these regions result in cell death or carcinogenesis. Towards these goals, we use an array of biophysical approaches including Nuclear Magnetic Resonance, crystallography and small-angle x-ray scattering. This diverse array of techniques will allow us to characterize both the dynamic and structural aspects of disordered regions. These biophysical observations will then be assessed for their functional consequences using in vivo techniques. The culmination of our research efforts will result in a complete understanding (structural and functional) of how phosphorylation of intrinsically disordered regions of protein regulate cellular processes.
Keywords - Biochemistry, Regulation of Intrinsically Disordered Proteins, RNA-binding Protein Dynamics and Structure, NMR, Crystallography