Kenan Distinguished Professor of Chemistry, UNC-CH
Joint Appointment Biochemistry and Biophysics & School of Medicine
Vice Chair of Facilities
Faculty Director of the UNC Macromolecular Interactions Facility
Co-faculty Director of the UNC Biomolecular NMR Facility
Member of Lineberger Comprehensive Cancer Center
(PhD in Biochemistry – Washington State University)
Accepting Rotation Students
HONORS & AWARDS
- Award for Excellence in Basic Science Mentoring, UNC Office of Graduate Education, 2019
- UNC Tanner Awards, Mentor Award for Lifetime Achievement, 2017
- Glen H. Elder, Jr. Distinguished Term Professor of Research and Undergraduate Education, 2013
- Vice Chair of Facilities for UNC Chemistry, 2013
- NIH Directors Pioneer Award, 2011
- Graduate Studies Committee, UNC Chemistry, 2010
My students and I use the formalisms of equilibrium thermodynamics and the tools of molecular biology and biophysics to understand the structure, stability, and function of globular and intrinsically-disordered proteins in physiologically relevant environments.
Pielak lab works in three areas:
High-resolution protein NMR studies in living cells.
Oxidative damage to α-synuclein, a key protein in Parkinson’s disease.
Pressure perturbation calorimetry of peptides and proteins.
My goal is to understand the chemistry of proteins as it occurs in living cells. This knowledge is fundamentally important and essential for ensuring that simple, inexpensive in vitro experiments can be used with confidence to diagnose and treat human disease. My lab has pioneered the study of both globular and disordered proteins under actual biologically relevant conditions both in vitro and in cells. We do this by developing innovative techniques to measure protein stability and diffusion in the presence of huge amounts of solutes that interfere with standard measurement techniques.
REPRESENTATIVE PUBLICATIONS (click for Full Publication List)
- Smith AE, Zhou Z, Pielak GJ. 2015. Hydrogen exchange of disordered proteins in Escherichia coli. Protein Science. 24: 706-713.
- Monteith WB, Cohen RD, Smith AE, Guzman-Cisneros E. 2015. Quinary structure modulates
- protein stability in cells. Proceedings of the National Academy of Sciences of the United States of America, 112: 1739-1742.
- Smith AE, Zhang Z, Pielak GJ, Li C 2015. NMR studicells and cell-like environments. Current Opinion in Structural Biology: 30: 7-16.
- Sarkar M, Pielak GJ. 2014. An osmolyte mitigates the destabilizing effect of protein crowding.Protein Science 23: 1161-1164. Cover article.
- Monteith WB, Pielak GJ. 2014. Residue level quantification of protein stability in living cells.Proceedings of the National Academy of Sciences of the United States of Americal: 111: 11335-11340. Featured by Faculty of 1000.
- Theillet F-X, Binolfi A, Frembgen-Kesner T, Hingorani K, Sarkar M, Kyne C, Li C, Crowley P, Gierasch L, Pielak G, Elcock A, Gershenson A, Selenko P. 2014. Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chemical Reviews 114: 6661-6714.
- Sarkar M, Lu J, Pielak GJ. 2014. Protein-crowder charge and protein stability. Biochemistry53:1601-1606.
- Xu G, Ye Y, Liu X, Cao S, Wu Q, Cheng K, Liu M, Pielak GJ, Li C. 2014. Strategies for protein NMR in Escherichia coli. Biochemistry 53: 1971-1981.
- Sarkar M, Smith AE, Pielak GJ. 2013. Impact of reconstituted cytosol on protein stability.Proceeding of the National Academy of Sciences of the United Sates of America 110:19342-19347. Featured by Faculty of 1000.
- Smith A, Sarkar M, Young G, Pielak GJ. 2013. Amide proton exchange of a dynamic loop in cell extracts. Protein Science 22:1313-1319.
- Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, Jiang L, Zhang X, Liu M, Pielak GJ, C Li C. 2013. 19F NMR as a probe of cytoplasmic viscosity and weak protein interactions in living cells.Chemistry–A European Journal 19: 12705-12710.
- Sarkar M, Li C, Pielak GJ. 2013. Soft interactions and crowding. Biophysical Reviews 5: 187-194.
- Tyrrell J, McGinnis JL, Weeks KM, & Pielak GJ (2013) The cellular environment stabilizes adenine riboswitch RNA structure. Biochemistry 52: 8777–8785. Featured by Faculty of 1000.
- Benton LA, Smith AE, Young GB, Pielak GJ. 2012. Unexpected effects of macromolecular crowding on protein stability. Biochemistry 51: 9773-9775.
- Wang, Y, Sarkar, M, Smith, AE, Krois, AS, Pielak, GJ. Macromolecular crowding and protein stability. Journal of the American Chemical Society 2012, 134, in press.
- Wang, Y, Benton, L, Singh, V, Pielak, GJ. Disordered protein diffusion under crowded conditions. Journal of Physical Chemistry Letters 2012, 3, in press.
- Pielak GJ, Tian F. 2012. Membrane proteins, magic-angle spinning, and in-cell NMR. Proceedings of the National Academy of Sciences of the United States of America 109: 4715-4716.
- Zigoneanu IG, Pielak GJ 2012. Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by 19F NMR. Molecular Pharmaceutics 9: 1024-1029.
- Zigoneanu IG, Yang YJ, Krois AS, Haque Md E, Pielak GJ. 2011. Interaction of α-synuclein and its A30P variant with vesicles of composition similar to mitochondrial membranes. Biochimica et Biophysica Acta 1818: 512-519.
- Fu R, Wang X, Li C, Santiago-Miranda A, Pielak GJ, Tian F. 2011. In situ Structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state MAS NMR. Journal of the American Chemical Society 133: 12370-12373.
- Schlesinger AP, Wang Y, Tadeo X, Millet O, Pielak GJ. 2011 Macromolecular crowding fails to fold a globular protein in cells.Journal of the American Chemical Society 133: 8082-8085.
- Miklos AC, Sarkar M, Li C, Pielak GJ. 2011. Proteins tune protein stability. Journal of the American Chemical Society 133: 7116–7120.
Lab Rooms: Genome 3250
Lab Fax: 919-962-6714