Research Topics
| G J PielakSummaryAffiliation: University of North Carolina Country: USA Publications
| Collaborators
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Detail Information
Publications
An upper limit for macromolecular crowding effectsAndrew C Miklos
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
BMC Biophys 4:13. 2011..abstract:..- Protein nuclear magnetic resonance under physiological conditionsGary J Pielak
Department of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 48:226-34. 2009.... - Woes of proline: a cautionary kinetic taleGary J Pielak
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
Protein Sci 15:393-4. 2006 - A model of intracellular organizationGary J Pielak
Department of Chemistry, Program in Molecular Biology and Biotechnology, and the Lineberger Cancer Research Center, University of North Carolina, Chapel Hill, NC 27599, USA
Proc Natl Acad Sci U S A 102:5901-2. 2005 - Interactions between yeast iso-1-cytochrome c and its peroxidaseG J Pielak
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 3290, USA
Biochemistry 40:422-8. 2001..Comparing these energies to the crystal structure of the complex leads to the conclusion that many of the substitutions induce a rearrangement of the complex... - Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theoryA S Morar
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 3290, USA
Biochemistry 40:281-5. 2001..None of the analyses are completely successful by themselves, and the results suggest that a complete analysis must account for both excluded-volume and chemical interactions... - Testing hypotheses about determinants of protein structure with high-precision, high-throughput stability measurements and statistical modelingFang Yi
Departments of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 42:7594-603. 2003..We see no correlation between the residuals derived from the full model and m(mut) - m(wt), and hence it is unlikely our m(mut) values reflect mutant-to-mutant differences in the denatured state... - Characterization of horse cytochrome c expressed in Escherichia coliC N Patel
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Protein Expr Purif 22:220-4. 2001..The expression system will help advance our understanding of the roles of cytochrome c in electron transfer, oxidative stress, and apoptosis by allowing the production of protein variants... - High-precision, high-throughput stability determinations facilitated by robotics and a semiautomated titrating fluorometerMarshall Hall Edgell
Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 42:7587-93. 2003.... - Second virial coefficients as a measure of protein--osmolyte interactionsG T Weatherly
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Protein Sci 10:12-6. 2001..We have interpreted the second virial coefficient as a measure of both excluded volume and protein--osmolyte binding. We conclude that simple models are not sufficient to understand the interactions between osmolytes and proteins... - Interpreting the effects of small uncharged solutes on protein-folding equilibriaP R Davis-Searles
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Annu Rev Biophys Biomol Struct 30:271-306. 2001..This phenomenon clearly has potential ramifications in the cell, where the crowded environment could well induce the same effects... - Crowding by trisaccharides and the 2:1 cytochrome c-cytochrome c peroxidase complexArtemiza S Morar
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290, USA
Biochemistry 41:547-51. 2002..Mutagenesis studies confirm that the second site includes Asp 148 on the peroxidase. Binding of both cytochrome c molecules is exothermic. The data are interpreted by assuming either the presence or absence of intersite interactions... - Protein (19)F NMR in Escherichia coliConggang Li
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
J Am Chem Soc 132:321-7. 2010..We also show that site-specific structural and dynamic information about both globular and disordered proteins can be obtained inside cells by using (19)F NMR... - Residue-level interrogation of macromolecular crowding effects on protein stabilityLisa M Charlton
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
J Am Chem Soc 130:6826-30. 2008..Our data reinforce the assertion that macromolecular crowding stabilizes the protein by destabilizing its unfolded states... - Stability and apoptotic activity of recombinant human cytochrome cAlina Olteanu
Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA
Biochem Biophys Res Commun 312:733-40. 2003..We use data from this assay along with data from the literature to define the apaf-1 binding site on human cytochrome c... - Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome cA S Morar
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Protein Sci 10:2195-9. 2001..Taken together, these data show that alpha-synuclein, a natively unfolded protein, is collapsed even in dilute solution, but lacks structure... - Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregationRebecca A S Ruf
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 47:13604-9. 2008..We also show that preformed oxidative aggregates are not incorporated into noncovalent fibrils. These data provide insight into how dityrosine may be formed in Lewy bodies seen in Parkinson's disease... - Searching for quantitative entropy-enthalpy compensation among protein variantsJames R Beasley
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599-3290, USA
Proteins 49:398-402. 2002..This study reinforces the idea that DeltaH-versus-DeltaS plots should not be used to provide evidence for SH compensation... - A bioreactor for in-cell protein NMRNaima G Sharaf
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
J Magn Reson 202:140-6. 2010..We have utilized the bioreactor to study the expression of the natively disordered protein alpha-synuclein, inside Escherichia coli cells... - Translational and rotational diffusion of a small globular protein under crowded conditionsConggang Li
Department of Chemistry, Department of Biochemistry and Biophysics, and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
J Phys Chem B 113:13390-2. 2009..We discuss our results in terms of other studies on the effects of macromolecules on globular protein diffusion... - Cytosol has a small effect on protein backbone dynamicsJulie E Bryant
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 45:10085-91. 2006..Increases in the time scale of both the picosecond and millisecond motions are observed, but the increases are less than approximately 30%... - Quantifying green fluorescent protein diffusion in Escherichia coli by using continuous photobleaching with evanescent illuminationKristin M Slade
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 3290, USA
J Phys Chem B 113:4837-45. 2009..We present the theoretical basis for the technique and demonstrate its applicability by measuring the diffusion coefficient, 6.3 +/- 1.1 microm(2)/s, of green fluorescent protein in Escherichia coli cells... - Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coliKristin M Slade
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 3290, USA
Biochemistry 48:5083-9. 2009..We conclude that expression of these soluble proteins has little to no effect on the diffusion of GFP. These results have implications for the utility of in-cell nuclear magnetic resonance spectroscopy... - Temperature-induced reversible conformational change in the first 100 residues of alpha-synucleinBrian C McNulty
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
Protein Sci 15:602-8. 2006..The properties of globular proteins change little with solution conditions until they denature cooperatively, but the properties of natively disordered proteins can vary dramatically with solution conditions... - Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorderBrian C McNulty
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
J Mol Biol 355:893-7. 2006.... - Protein dynamics in living cellsJulie E Bryant
Departments of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 44:9275-9. 2005..Therefore, it appears that dilute solution steady-state {1H}-15N nOe measurements provide biologically relevant information about pico- to nanosecond backbone motion in proteins... - Impact of protein denaturants and stabilizers on water structureJoseph D Batchelor
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
J Am Chem Soc 126:1958-61. 2004..Our results indicate that efforts to explain solute effects should focus on other hypotheses, including those based on preferential interaction and excluded volume... - Effects of proteins on protein diffusionYaqiang Wang
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
J Am Chem Soc 132:9392-7. 2010..In summary, weak but nonspecific, noncovalent chemical interactions between proteins appear to fundamentally impact protein diffusion in cells... - 19F NMR studies of alpha-synuclein conformation and fibrillationConggang Li
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Biochemistry 48:8578-84. 2009..We conclude that 19F NMR spectroscopy is useful for obtaining residue-level, quantitative information about the structure, binding, and aggregation of alpha-synuclein... - Volume exclusion and soft interaction effects on protein stability under crowded conditionsAndrew C Miklos
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA
Biochemistry 49:6984-91. 2010..We conclude that the role of native-state binding and other soft interactions needs to be seriously considered when applying both theory and experiment to studies of macromolecular crowding... - FlgM gains structure in living cellsMatthew M Dedmon
Departments of Chemistry, and Biochemistry and Biophysics, and Lineberger Cancer Research Center, University of North Carolina, Chapel Hill, NC 27599, USA
Proc Natl Acad Sci U S A 99:12681-4. 2002.... - Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditionsConggang Li
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
J Am Chem Soc 131:1368-9. 2009..We describe a simple and reliable NMR method to distinguish viscosity effects from binding and aggregation under crowded conditions... - Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopyConggang Li
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
J Am Chem Soc 130:6310-1. 2008..From in vitro studies we conclude that this difference in detectability is the result of the differential dynamical response of disordered and ordered proteins to the changes of motion caused by the increased viscosity in cells... - Peeking into living eukaryotic cells with high-resolution NMRLisa M Charlton
Department of Chemistry and Biochemistry, Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, NC 27599, USA
Proc Natl Acad Sci U S A 103:11817-8. 2006 - Effects of molecular crowding by saccharides on alpha-chymotrypsin dimerizationChetan N Patel
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
Protein Sci 11:997-1003. 2002.... - Development and cardiac contractility: cardiac troponin T isoforms and cytosolic calcium in rabbitShannon J McCall
Department of Pathology, Duke University Medical Center, Durham, NC 27710, USA
Pediatr Res 60:276-81. 2006..2 +/- 1.6 pA/pF). The higher calcium sensitivity of Tn-Ca binding and of force development conferred by rcTnT(1) suggest that higher neonatal cTnT(1) expression may partially compensate for the lower systolic [Ca(2+)](i)... - Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complexGregory Engstrom
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, USA
Biochemistry 42:2816-24. 2003..The interaction of yeast Ru-39-Cc with yeast cytochrome bc1 is stronger than that of horse Ru-39-Cc with bovine cytochrome bc1, suggesting that nonpolar interactions are stronger in the yeast system... - Reconsideration of sedimentation equilibrium distributions reflecting the effects of small inert cosolutes on the dimerization of alpha-chymotrypsinDonald J Winzor
Department of Biochemistry, University of Queensland, Brisbane, Queensland 4072, Australia
Biophys Chem 130:89-92. 2007..Support is thereby provided for the earlier contention that the effect of sucrose, as well as of glucose and raffinose, on dimerization may be rationalized quantitatively in terms of molecular crowding by an inert cosolute...