Jun Zhang. Assistant Professor
Chemistry Building 266
(205) 934-2139

Research and Teaching Interests: Biochemistry, Regulation of Intrinsically Disordered Proteins, RNA-binding Protein Dynamics and Structure, NMR, Crystallography

Office Hours: By appointment

  • PhD, University of North Carolina at Chapel Hill

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.

Research Opportunities

We are looking for talented, motivated individuals (PhD students, postdocs, and undergrads) to join our research group. If you are interested in our lab, please send me an email. Include your curriculum vitae and a description of your research interests.
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.

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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.
  • CH 700: Foundations of Physical and Analytical Chemistry
  • Zhang, J.; Gonzalez, LE; Hall, TMT. Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. Nucleic Acid Research 2016, doi: 10.1093/nar/gkw961.
  • Zhang, J.; McCann, KL; Qiu, C; Gonzalez, LE; Baserga, SJ; Hall, TMT. Nop9, a new PUF-like protein regulates pre-rRNA cleavage events to produce mature 18S rRNA. Nature Communications 2016, 7:13085.
  • Zhang, J.; Tan, D.Z.; DeRose, E.F.; Perera, L.; Dominski, Z.; Marzluff, W.F.; Tong, L.; Hall, T.M.T. Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. Proc. Natl. Acad. Sci. USA 2014, 111(29): E2937-E2946.
  • Zhang, J.; Lewis, S.; Kuhlman, B.; Lee, AL. Supertertiary structure of the MAGUK core from PSD-95. Structure 2013, 21 (3):402-13.
  • Zhang. J.; Petit, C.M.; King, D.S.; Lee A.L. Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK). J. Biol. Chem. 2011, 286(48):41776-85.
  • Zhang, J.; Sapienza, P.J.; Ke, H.M.; Chang, A.; Hengel, S.R.; Wang, H.C.; Philips, G.N.; Lee, A.L. Crystallographic and NMR evaluation of the impact of peptide binding to the second PDZ domain of PTP1E. Biochemistry 2010, 49 (43), 9280-91.
  • Petit, C.M., Zhang, J.; Sapienza, P.J.; Fuentes, E.J.; Lee, A.L. Hidden dynamic allostery in a PDZ domain. Proc. Natl. Acad. Sci. USA 2009; 106(43):18249-54.
  • Yan, Y.B.; Zhang, J.; He, H.W.; Zhou, H.M. Oligomerization and aggregation of bovine pancreatic ribonuclease A: characteristic events observed by FTIR spectroscopy. Biophys. J. 2006; 90(7):2525-33. Epub 2006 Jan. 13.
  • Zhang, J.; Yan, Y.B. Probing conformational changes of proteins by quantitative second-derivative infrared spectroscopy. Analytical Biochemistry 2005; 340(1):89-98.