G
Gary J. Pielak
Researcher at University of North Carolina at Chapel Hill
Publications - 202
Citations - 9963
Gary J. Pielak is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Macromolecular crowding & Globular protein. The author has an hindex of 50, co-authored 185 publications receiving 8755 citations. Previous affiliations of Gary J. Pielak include University of British Columbia & University of Oxford.
Papers
More filters
Journal ArticleDOI
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).
Francois Xavier Theillet,Andres Binolfi,Tamara Frembgen-Kesner,Karan S. Hingorani,Mohona Sarkar,Ciara Kyne,Conggang Li,Peter B. Crowley,Lila M. Gierasch,Gary J. Pielak,Adrian H. Elcock,Anne Gershenson,Philipp Selenko +12 more
TL;DR: This work has learned about the unexpected intracellular stability of disordered proteins, their roles in integrating post-translational protein modifications in cell signaling and about their functions in regulatory processes ranging from transcription to cell fate decisions.
Journal ArticleDOI
Impact of protein denaturants and stabilizers on water structure.
TL;DR: It is found that there is no correlation between a solute's impact on water structure and its effect on protein stability, indicating that efforts to explain solute effects should focus on other hypotheses, including those based on preferential interaction and excluded volume.
Journal ArticleDOI
FlgM gains structure in living cells
TL;DR: NMR is used to show that FlgM gains structure inside living Escherichia coli cells and under physiologically relevant conditions in vitro, i.e., in solutions containing high concentrations of glucose, BSA, or ovalbumin.
Journal ArticleDOI
Macromolecular Crowding and Protein Stability
TL;DR: The results show that both chemical interactions and hard-core repulsions must be considered when assessing the effects of crowding and help explain previous observations about protein stability and dynamics in cells.
Journal ArticleDOI
Interpreting the effects of small uncharged solutes on protein-folding equilibria.
TL;DR: Experimental advantage may still be taken of the ability of the cosolute effect to promote not only protein stabilization but also protein self-association and complex formation between dissimilar reactants.