Gary J. Pielak (born July 17, 1955) is an American biological chemist who is known for developing 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]
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 Nobel Prize-winner Michael Smith and at the University of Oxford with Robert J.P. Williams. [11] He joined the Department of Chemistry at the University of North Carolina at Chapel Hill in 1989. [11]
Using in-cell nuclear magnetic resonance spectroscopy, a technique he helped develop, [12] 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. [13] [14] [15] [16] For his work in this area, he received an NIH Director's Pioneer Award in 2006. [17]
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 [18] . He was an invited speaker at the 2017 Nobel Symposium on Protein Folding: From Mechanisms to Impact on Cells, in Stockholm, Sweden. [19]
In 2023, Pielak received both the Johnston Teaching Excellence Award and the Faculty Award for Excellence in Doctoral Mentoring [20] 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. [21]
"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. [22]
"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. [23]
"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. [24]
"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. [25]
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The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion where it plays a critical role in cellular respiration. It transfers electrons between Complexes III and IV. Cytochrome c is highly water-soluble, unlike other cytochromes. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It also plays a major role in cell apoptosis. In humans, cytochrome c is encoded by the CYCS gene.
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A chaotropic agent is a molecule in water solution that can disrupt the hydrogen bonding network between water molecules. This has an effect on the stability of the native state of other molecules in the solution, mainly macromolecules by weakening the hydrophobic effect. For example, a chaotropic agent reduces the amount of order in the structure of a protein formed by water molecules, both in the bulk and the hydration shells around hydrophobic amino acids, and may cause its denaturation.
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Molecular biophysics is a rapidly evolving interdisciplinary area of research that combines concepts in physics, chemistry, engineering, mathematics and biology. It seeks to understand biomolecular systems and explain biological function in terms of molecular structure, structural organization, and dynamic behaviour at various levels of complexity. This discipline covers topics such as the measurement of molecular forces, molecular associations, allosteric interactions, Brownian motion, and cable theory. Additional areas of study can be found on Outline of Biophysics. The discipline has required development of specialized equipment and procedures capable of imaging and manipulating minute living structures, as well as novel experimental approaches.
Harry Barkus Gray is the Arnold O. Beckman Professor of Chemistry at California Institute of Technology.
The phenomenon of macromolecular crowding alters the properties of molecules in a solution when high concentrations of macromolecules such as proteins are present. Such conditions occur routinely in living cells; for instance, the cytosol of Escherichia coli contains about 300–400 mg/ml of macromolecules. Crowding occurs since these high concentrations of macromolecules reduce the volume of solvent available for other molecules in the solution, which has the result of increasing their effective concentrations. Crowding can promote formation of a biomolecular condensate by colloidal phase separation.
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