Gary J. Pielak

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Gary J. Pielak (born July 17, 1955) is an American biological chemist, who is known for pioneering quantitative techniques for measuring protein structure, stability, diffusion, and concentration in living cells, and under crowded conditions.

Pielak is the Kenan Distinguished Professor.[1] of Chemistry, Biochemistry and Biophysics at the University of North Carolina at Chapel Hill School of Medicine[2], Lineberger Comprehensive Cancer Center[3], and Department of Chemistry[4]. He is a Fellow of the Biophysical Society[5][6].

Education[edit]

Pielak earned a B.A. in chemistry, cum laude, from Bradley University in 1977, and a Ph.D. in biochemistry 1983 from Washington State University under J. Ivan Legg.[7] His dissertation was titled "Characterization of Arsanilazo & Sulfanilazo Proteins".[7] He conducted postdoctoral work studying the functional role of certain amino acid residues on cytochrome c electron transfer[8][9][10] at the University of British Columbia with eventual Nobel Prize-winner Michael Smith and at the University of Oxford with Robert Williams.[11] He joined the Department of Chemistry at the University of North Carolina at Chapel Hill in 1989.[11]

Research[edit]

Using in-cell nuclear magnetic resonance spectroscopy, a technique he helped develop,[citation needed] Pielak determined that the effects of in-cell crowding do not arise solely from the close-packed nature of the cytoplasm but rather that repulsive and attractive chemical interactions between cellular components determine the effects of macromolecular crowding. These interactions organize the inside of cells, controlling metabolism and signaling. He and his collaborators have presented a quantitative model to explain crowding effects that is independent of crowder identity.[12][13][14][15] For his work in this area, he received an NIH Director's Pioneer Award in 2006.[16]

Selected honors[edit]

Gary Pielak has been on the Editorial Advisory Board of the journal Protein Science, and serves on the Editorial Board of the journal Magnetic Resonance Letters[17]. He was an invited speaker at the 2017 Nobel Symposium on Protein Folding: From Mechanisms to Impact on Cells, in Stockholm, Sweden.[18]

In 2023, Pielak received both the Johnston Teaching Excellence Award and the Faculty Award for Excellence in Doctoral Mentoring[19] from the University of North Carolina at Chapel Hill. He also presented the McElvain Lecture at the University of Wisconsin, Madison that year.[citation needed] In 2024, he was an invited speaker at Protein Folding Dynamics Gordon Research Conference in Galveston, Texas.[20]

Selected publications[edit]

"Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)" (2014). Francois-Xavier Theillet, Andres Binolfi, Tamara Frembgen-Kesner, Karan Hingorani, Mohona Sarkar, Ciara Kyne, Conggang Li, Peter B Crowley, Lila Gierasch, Gary J Pielak, Adrian H Elcock, Anne Gershenson, Philipp Selenko. Chemical Reviews 114 (13), 6661-6714.[21]

"FlgM gains structure in living cells" (2002). Matthew M Dedmon, Chetan N Patel, Gregory B Young, Gary J Pielak, Proceedings of the National Academy of Sciences 99 (20), 12681-12684.[22]

"Impact of Protein Denaturants and Stabilizers on Water Structure" (2004). Joseph D. Batchelor, Alina Olteanu, Ashutosh Tripathy, and Gary J. Pielak, J. Am. Chem. Soc. 2004, 126, 7, 1958–1961.[23]

"Macromolecular Crowding and Protein Stability" (2012). Yaqiang Wang, Mohona Sarkar, Austin E. Smith, Alexander S. Krois, and Gary J. Pielak, J. Am. Chem. Soc. 2012, 134, 40, 16614–16618.[24]

References[edit]

  1. ^ "University Distinguished Professors". Provost & Chief Academic Officer - UNC Chapel Hill. Retrieved 2024-03-21.
  2. ^ "Gary Pielak". Biochemistry and Biophysics. Retrieved 2024-04-09.
  3. ^ "Gary Pielak". UNC Lineberger. Retrieved 2024-04-09.
  4. ^ "Pielak, Gary". Retrieved 2024-04-09.
  5. ^ Clabo, Carolyn (2023-09-22). "Dr. Gary Pielak named 2024 Biophysical Society Fellow". Biochemistry and Biophysics. Retrieved 2024-03-21.
  6. ^ "Pielak elected 2024 Biophysical Society Fellow". Retrieved 2024-04-09.
  7. ^ a b Gary J. Pielak (22 April 2024). "Curriculum Vitae" (PDF). Pielak Group. Archived from the original (PDF) on 31 May 2024. Retrieved 31 May 2024.
  8. ^ Pielak, Gary J.; Mauk, A. Grant; Smith, Michael (1985). "Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function". Nature. 313 (5998): 152–154. doi:10.1038/313152a0. Retrieved 31 May 2024.
  9. ^ Pielak, Gary J.; Coricar, David W.; Moore, Geoffrey R.; Williams, Robert J. P. (1987). "The structure of cytochrome c and its relation to recent studies of long-range electron transfer". Protein Engineering, Design and Selection. 1 (2): 83–88. doi:10.1093/protein/1.2.83. Retrieved 31 May 2024.
  10. ^ Pielak, Gary J.; Boyd, Jonathan; Moore, Geoffrey R.; Williams, Robert J. P. (1988). "Proton‐NMR studies show that the Thr‐102 mutant of yeast iso‐1‐cytochrome c is a typical member of the eukaryotic cytochrome c family". European Journal of Biochemistry. 177 (1): 167–177. doi:10.1111/j.1432-1033.1988.tb14359.x-i2. PMID 2846294. Retrieved 31 May 2024.
  11. ^ a b "Pielak Research Group". pielakgroup.web.unc.edu. Archived from the original on 31 May 2024. Retrieved 31 May 2024.
  12. ^ Stewart, Claire J.; Olgenblum, Gil I.; Propst, Ashlee; Harries, Daniel; Pielak, Gary J. (2023-01-23) [January 23, 2023]. "Resolving the enthalpy of protein stabilization by macromolecular crowding". Protein Science. 32 (3): e4573. doi:10.1002/pro.4573. ISSN 0961-8368. PMC 9942490. PMID 36691735.
  13. ^ Guseman, Alex J.; Pielak, Gary J. (2019), Ito, Yutaka; Dötsch, Volker; Shirakawa, Masahiro (eds.), "Chapter 12. Protein Stability and Weak Intracellular Interactions", New Developments in NMR, Cambridge: Royal Society of Chemistry, pp. 188–206, doi:10.1039/9781788013079-00188, ISBN 978-1-78801-217-1, S2CID 213364320, retrieved 2024-03-13
  14. ^ Pielak, Gary (March 1, 2021). "Dynamical spectroscopy and microscopy of proteins in cells". Current Opinion in Structural Biology. 70: 1–7. doi:10.1016/j.sbi.2021.02.001. PMID 33662744 – via Elsevier Science Direct.
  15. ^ Speer, Shannon L.; Stewart, Claire J.; Sapir, Liel; Harries, Daniel; Pielak, Gary J. (2022-05-09). "Macromolecular Crowding Is More than Hard-Core Repulsions". Annual Review of Biophysics. 51 (1): 267–300. doi:10.1146/annurev-biophys-091321-071829. ISSN 1936-122X. PMID 35239418.
  16. ^ "2006 Awardees | NIH Common Fund". commonfund.nih.gov. Retrieved 2024-03-21.
  17. ^ https://www.sciencedirect.com/journal/magnetic-resonance-letters/about/editorial-board
  18. ^ "Protein folding: Much more intricate than we thought". Chemical & Engineering News. Retrieved 2024-03-13.
  19. ^ "Faculty Award for Excellence in Doctoral Mentoring". University of North Carolina Graduate School.
  20. ^ "2024 Protein Folding Dynamics Conference GRC". grc.org. 2024. Archived from the original on 31 May 2024. Retrieved 31 May 2024.
  21. ^ Theillet, Francois-Xavier; Binolfi, Andres; Frembgen-Kesner, Tamara; Hingorani, Karan; Sarkar, Mohona; Kyne, Ciara; Li, Conggang; Crowley, Peter B.; Gierasch, Lila; Pielak, Gary J.; Elcock, Adrian H.; Gershenson, Anne; Selenko, Philipp (2014-07-09). "Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)". Chemical Reviews. 114 (13): 6661–6714. doi:10.1021/cr400695p. ISSN 0009-2665. PMC 4095937. PMID 24901537.
  22. ^ Dedmon, Matthew M.; Patel, Chetan N.; Young, Gregory B.; Pielak, Gary J. (2002-09-23). "FlgM gains structure in living cells". Proceedings of the National Academy of Sciences. 99 (20): 12681–12684. Bibcode:2002PNAS...9912681D. doi:10.1073/pnas.202331299. ISSN 0027-8424. PMC 130520. PMID 12271132.
  23. ^ Batchelor, Joseph D.; Olteanu, Alina; Tripathy, Ashutosh; Pielak, Gary J. (2004-02-01). "Impact of Protein Denaturants and Stabilizers on Water Structure". Journal of the American Chemical Society. 126 (7): 1958–1961. doi:10.1021/ja039335h. ISSN 0002-7863. PMID 14971928.
  24. ^ Wang, Yaqiang; Sarkar, Mohona; Smith, Austin E.; Krois, Alexander S.; Pielak, Gary J. (2012-10-10). "Macromolecular Crowding and Protein Stability". Journal of the American Chemical Society. 134 (40): 16614–16618. doi:10.1021/ja305300m. ISSN 0002-7863. PMID 22954326.
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