Gary Pielak, PhD


  • NIH Directors Pioneer Award
  • Glen H. Elder, Jr. Distinguished Term Professor of Research and Undergraduate Education



My goal is to understand the chemistry of biopolymers 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 uncover the fundamentals of biology as well as to diagnose and treat human disease.

Cells contain an exceptionally complex array of macromolecules at concentrations exceeding 300 g/L. The natural, most relevant state of a biological macromolecule is thus a "crowded" one. Such crowding has been predicted to impact rates and equilibria dramatically, and it is likely that some parameters measured in dilute solution – especially those relating to ligand binding, intermolecular association, and folding equilibria – differ by orders of magnitude from biologically relevant values in cells. Moving quantitative biophysics from dilute solution to the inside of living cells represents a major frontier of biomedical research.

Core Techniques:

Nuclear magnetic resonance spectroscopy, Circular dichroism spectropolarimetry, Analytical ultracentrifugation


    • 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.


      C742 Kenan Labs
      Campus Box # 3290
      Chapel Hill, NC 27599

      Office: 919-966-3671
      Fax: 919-962-2388

      Pielak Lab Website