Gary Pielak

Research: Protein biophysics in-vitro and in-vivo

Gary Pielak

 Kenan Distinguished Professor of Chemistry, UNC-CH

Joint Appointment Biochemistry and Biophysics

Faculty Director of the UNC Macromolecular Interactions Facility

Co-faculty Director of the UNC Biomolecular NMR Facility

Member of Lineberger Comprehensive Cancer Center

PhD - Washington State University

3250 Genome Sciences Building
Chapel Hill, NC 27599-7260

Pielak Lab Website


  • 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 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  PubMed(click for Full Publication List)


  • Wang, Y, Benton, L, Singh, V, Pielak, GJ. Disordered protein diffusion under crowded conditions. Journal of Physical Chemistry Letters 20123, 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 Contact:

Lab Rooms: Genome 3250

Lab Fax: 919-962-6714

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