G. Pielak

发表

Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)

L. Gierasch, A. Elcock, Conggang Li, 2014, Chemical reviews.

Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy

Conggang Li, Maili Liu, G. Pielak, 2017, Analytical and Bioanalytical Chemistry.

Rapid Quantification of Protein-Ligand Binding via 19F NMR Lineshape Analysis.

G. Pielak, C. Waudby, Samantha S. Stadmiller, 2020, Biophysical journal.

Protein crowding tunes protein stability.

Andrew C. Miklos, Mohona Sarkar, G. Pielak, 2011, Journal of the American Chemical Society.

Interactions between yeast iso-1-cytochrome c and its peroxidase.

G. Pielak, X. Wang, 2001, Biochemistry.

Crowding by trisaccharides and the 2:1 cytochrome c-cytochrome c peroxidase complex.

G. Pielak, A. S. Morar, 2002, Biochemistry.

Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by ¹⁹F NMR.

G. Pielak, I. G. Zigoneanu, 2012, Molecular pharmaceutics.

Positively Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR.

Conggang Li, Maili Liu, G. Pielak, 2019, The journal of physical chemistry. B.

Macromolecular crowding fails to fold a globular protein in cells.

G. Pielak, O. Millet, Yaqiang Wang, 2011, Journal of the American Chemical Society.

Hydrogen exchange of disordered proteins in Escherichia coli

G. Pielak, Austin E. Smith, L. Z. Zhou, 2015, Protein science : a publication of the Protein Society.

An upper limit for macromolecular crowding effects

Andrew C. Miklos, Conggang Li, G. Pielak, 2011, BMC biophysics.

Protein-Peptide Binding Energetics under Crowded Conditions.

G. Pielak, Samantha S. Stadmiller, Jhoan S Aguilar, 2020, The journal of physical chemistry. B.

Unexpected effects of macromolecular crowding on protein stability.

G. Pielak, G. B. Young, Austin E. Smith, 2012, Biochemistry.

Crowding and function reunite

Andrew C. Miklos, G. Pielak, Andrew C Miklos, 2010, Proceedings of the National Academy of Sciences.

Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR† †Electronic supplementary information (ESI) available: 1D 19F NMR and 2D 1H–15N HSQC spectra. See DOI: 10.1039/c5sc04297f

Conggang Li, Maili Liu, G. Pielak, 2015, Chemical science.

Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position.

G J Pielak, G. Brayer, G. Louie, 1988, Biochemistry.

Structural studies of yeast iso-1 cytochrome c mutants by resonance Raman spectroscopy.

R. J. Williams, G. Pielak, P. Hildebrandt, 1991, European journal of biochemistry.

Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiae.

R. J. Williams, G. Pielak, J. Boyd, 1991, Biochemistry.

Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c.

R. J. Williams, G. Pielak, J. Boyd, 1990, Biochemistry.

Protecting activity of desiccated enzymes

S. Neher, G. Pielak, Thomas C Boothby, 2019, Protein science : a publication of the Protein Society.

Interaction of α-synuclein with vesicles that mimic mitochondrial membranes.

A. Krois, G. Pielak, I. G. Zigoneanu, 2012, Biochimica et biophysica acta.

Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase (*)

G. Pielak, L. Geren, B. Durham, 1995, The Journal of Biological Chemistry.

Macromolecular and Small Molecular Crowding Have Similar Effects on α-Synuclein Structure.

Conggang Li, Maili Liu, G. Pielak, 2017, Chemphyschem : a European journal of chemical physics and physical chemistry.

Dynamical spectroscopy and microscopy of proteins in cells.

M. Gruebele, G. Pielak, 2021, Current opinion in structural biology.

High-Throughput, Precise Protein Stability Measurements Facilitated by Robotics

M. Edgell, G. Pielak, Fang Yi, 2005 .

Residue-level interrogation of macromolecular crowding effects on protein stability.

Conggang Li, G. Pielak, C. Barnes, 2008, Journal of the American Chemical Society.

Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts.

R. J. Williams, G. Pielak, J. Boyd, 1991, Biochemistry.

The intracellular environment affects protein–protein interactions

Conggang Li, Maili Liu, G. Pielak, 2021, Proceedings of the National Academy of Sciences.

High-precision, high-throughput stability determinations facilitated by robotics and a semiautomated titrating fluorometer.

M. Edgell, G. Pielak, Fang Yi, 2003, Biochemistry.

Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase.

M. Miller, G. Pielak, L. Geren, 1996, Biochemistry.

Desiccation‐tolerance and globular proteins adsorb similar amounts of water

G. Pielak, Julia A. Brom, Julia A Brom, 2022, Protein science : a publication of the Protein Society.

Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site.

G. Pielak, B. Durham, F. Millett, 1996, Biochemistry.

Protein NMR under Physiological Conditions †

Andrew C. Miklos, Guifang Wang, Conggang Li, 2009 .

Alpha-Synuclein Conformation Affects Its Tyrosine Dependent Oxidative Aggregation

G. Pielak, I. G. Zigoneanu, Rebecca A. S. Ruf, 2009 .

α-synuclein C-terminal Truncation Modulates Its Cytotoxicity and Aggregation by Promoting Its N-terminal Interactions With Membrane and Chaperone

Xiaoxia Zhou, Zeting Zhang, Conggang Li, 2022 .

Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c.

S. Sligar, G. Pielak, B. Durham, 1993, Biochemistry.

Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex.

B. Trumpower, G. Pielak, K. Xiao, 2003, Biochemistry.

Elimination of the negative soret Cotton effect of cytochrome c by replacement of the invariant phenylalanine using site-directed mutagenesis

C. Kay, G. Pielak, A. Mauk, 1986 .

Factors Controlling the Rates of Electron Transfer in Proteins

G. Pielak, Yuan Gao, Robert J.P. Williams, 1988 .

Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-linking.

T. Poulos, G. Pielak, A. Saunders, 1996, Biochemistry.

Membrane‐mediated disorder‐to‐order transition of SNAP25 flexible linker facilitates its interaction with syntaxin‐1 and SNARE‐complex assembly

Zeting Zhang, Conggang Li, Maili Liu, 2019, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

19 F-NMR Studies of α -Synuclein Conformation and Fibrillation†

Guifang Wang, Conggang Li, G. Pielak, 2013 .

Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.

G. Pielak, Samantha Piszkiewicz, Julia A. Brom, 2021, Biochemistry.

In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR.

Riqiang Fu, Xingsheng Wang, Conggang Li, 2011, Journal of the American Chemical Society.

Membrane proteins, magic-angle spinning, and in-cell NMR

G. Pielak, Fang Tian, 2012, Proceedings of the National Academy of Sciences.

Stability and apoptotic activity of recombinant human cytochrome c.

G. Pielak, M. Linhoff, Matthew M Dedmon, 2003, Biochemical and biophysical research communications.

The role of the internal hydrogen bond network in first-order protein electron transfer between Saccharomyces cerevisiae iso-1-cytochrome c and bovine microsomal cytochrome b5.

R. J. Williams, F. Sherman, G. Pielak, 1991, European journal of biochemistry.

C-terminal truncation modulates α-Synuclein’s cytotoxicity and aggregation by promoting the interactions with membrane and chaperone

Xiaoxia Zhou, Zeting Zhang, Maili Liu, 2022, Communications Biology.

The Expanding Zoo of In-Cell Protein NMR.

G. Pielak, Samantha S. Stadmiller, 2018, Biophysical journal.

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.

R. J. Williams, G. Moore, G. Pielak, 1988, European journal of biochemistry.

The role of phenylalanine-82 in electron-exchange reactions of eukaryotic cytochromes c

G. Pielak, D. Whitford, ROBERT J. P. Williams, 1991 .

Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c.

G. Pielak, B. Hoffman, A. Mauk, 1988, Science.

The structure of cytochrome c and its relation to recent studies of long-range electron transfer.

R. J. Williams, G. Moore, G. Pielak, 1987, Protein engineering.

Quantification of azo-coupled lysine in azo proteins by amino acid analysis.

G. Pielak, S. Gurusiddaiah, J. I. Legg, 1986, Analytical biochemistry.

Preparation and Characterization of Sulfanilazo and Arsanilazo Proteins

G. Pielak, M. Urdea, J. I. Legg, 1984 .

Rheostatic control of protein expression using Tuner™ cells.

G. Pielak, Shannon L. Speer, I. Chu, 2020, Biochemistry.

Controlling and quantifying protein concentration in Escherichia coli

Brandie M. Ehrmann, G. Pielak, Alex J. Guseman, 2019, Protein science : a publication of the Protein Society.

Impact of protein denaturants and stabilizers on water structure.

G. Pielak, A. Tripathy, J. Batchelor, 2004, Journal of the American Chemical Society.

Toxicity and Immunogenicity of a Tardigrade Cytosolic Abundant Heat Soluble Protein in Mice

G. Pielak, Samantha Piszkiewicz, Brooke E. Christian, 2020, Frontiers in Pharmacology.

Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein.

G. Pielak, A. Mauk, M. Smith, 1987, Protein engineering.

Probing the Micelle‐Bound Aggregation‐Prone State of α‐Synuclein with 19F NMR Spectroscopy

Guifang Wang, G. Pielak, Conggang Li , 2010, Chembiochem : a European journal of chemical biology.

Partially formed native tertiary interactions in the A-state of cytochrome c.

G. Pielak, D. Hostetter, P. Hardwidge, 1999, Journal of molecular biology.

Baseline length and automated fitting of denaturation data

G. Pielak, Devon L. Allen, 1998, Protein science : a publication of the Protein Society.

Crowding and Confinement Can Oppositely Affect Protein Stability.

Zeting Zhang, Conggang Li, Maili Liu, 2018, Chemphyschem : a European journal of chemical physics and physical chemistry.

Second virial coefficients as a measure of protein–osmolyte interactions

G. Pielak, G. Weatherly, 2001, Protein science : a publication of the Protein Society.

Native tertiary structure in an A-state.

G. Pielak, M. Lehti, J. Marmorino, 1998, Journal of molecular biology.

Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state.

S. Betz, G. Pielak, 1992, Biochemistry.

Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c

G. Moore, G. Pielak, A. Davies, 1991, FEBS letters.

The cellular environment stabilizes adenine riboswitch RNA structure.

K. Weeks, Jennifer L. McGinnis, G. Pielak, 2013, Biochemistry.

Development and Cardiac Contractility: Cardiac Troponin T Isoforms and Cytosolic Calcium in Rabbit

S. McCall, G. Pielak, R. Solaro, 2006, Pediatric Research.

Pressure perturbation calorimetry of helical peptides

Devin G. Barrett, T. Creamer, G. Pielak, 2005, Proteins.

Protein Stability in Reverse Micelles.

G. Pielak, Austin E. Smith, Michael Senske, 2016, Angewandte Chemie.

Interpreting the effects of small uncharged solutes on protein-folding equilibria.

D. Erie, D. Winzor, G. Pielak, 2001, Annual review of biophysics and biomolecular structure.

Protein (19)F NMR in Escherichia coli.

Guifang Wang, Conggang Li, G. Pielak, 2010, Journal of the American Chemical Society.

19F NMR studies of alpha-synuclein conformation and fibrillation.

Guifang Wang, Conggang Li, G. Pielak, 2009, Biochemistry.

Azo Protein Analogues: Synthesis and Characterization of Arsanilazo and Sulfanilazo Derivatives of Tyrosine and Histidine

G. Pielak, M. Urdea, K. Igi, 1984 .

Strategies for protein NMR in Escherichia coli.

Conggang Li, Maili Liu, G. Pielak, 2014, Biochemistry.

Cosolute and Crowding Effects on a Side-By-Side Protein Dimer.

G. Pielak, Alex J. Guseman, 2017, Biochemistry.

NMR studies of protein folding and binding in cells and cell-like environments.

Zeting Zhang, Conggang Li, G. Pielak, 2015, Current opinion in structural biology.

A genetic approach for identifying critical residues in the fingers and palm subdomains of HIV-1 reverse transcriptase.

G J Pielak, C. Hutchison, J. Wrobel, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Translational and rotational diffusion of a small globular protein under crowded conditions.

Conggang Li, Conggang Li, G. Pielak, 2009, The journal of physical chemistry. B.

Challenge of mimicking the influences of the cellular environment on RNA structure by PEG-induced macromolecular crowding.

K. Weeks, G. Pielak, J. Tyrrell, 2015, Biochemistry.

Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine.

G. Pielak, Samantha S. Stadmiller, Alex J. Guseman, 2017, Journal of molecular biology.

Osmolyte-induced changes in protein conformational equilibria.

D. Allen, D. Erie, G. Pielak, 2000, Biopolymers.

FlgM gains structure in living cells

G. Pielak, Matthew M Dedmon, G. B. Young, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Characterization of horse cytochrome c expressed in Escherichia coli.

G. Pielak, C. N. Patel, M. C. Lind, 2001, Protein expression and purification.

Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.

D. Koshland, G. Pielak, L. Rebecchi, 2017, Molecular cell.

Tardigrades use intrinsically disordered proteins to survive desiccation

Rohit V. Pappu, Gary J. Pielak, Alex S. Holehouse, 2018, Cryobiology.

Site-directed mutagenesis of the histidine heme ligand in iso-1-cytochrome c of Saccharomyces cerevisiae

G. Pielak, T. N. Sorrell, Z. Fredericks, 1992 .

Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function

G. Pielak, Michael B. Smith, A. Mauk, 1985, Nature.

A model of intracellular organization

G. Pielak, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Macromolecular Crowding in the Escherichia coli Periplasm Maintains α-Synuclein Disorder

Gary J. Pielak, G. Pielak, G. B. Young, 2006 .

Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder.

G. Pielak, G. B. Young, Gary J Pielak, 2006, Journal of molecular biology.

Erratum (Retracted article): Protein dynamics in living cells (Biochemistry (2005) 44, 26, (9275-9279))

Andrew L. Lee, Gary J. Pielak, G. Pielak, 2007 .

Protein dynamics in living cells.

Andrew L. Lee, G. Pielak, G. B. Young, 2005, Biochemistry.

Solvent‐induced collapse of α‐synuclein and acid‐denatured cytochrome c

Gary J. Pielak, G. Pielak, A. S. Morar, 2001 .

Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c.

G J Pielak, G. Pielak, A. S. Morar, 2001, Protein science : a publication of the Protein Society.

Emergence of life: Physical chemistry changes the paradigm

B. Poolman, G. Pielak, J. Spitzer, 2015, Biology Direct.

Design, synthesis, expression, and characterization of the genes for mouse FcγRIIb1 and FcγRIIb2 cytoplasmic regions

N. Thompson, G. Pielak, Lixin Chen, 1997, Protein science : a publication of the Protein Society.

In-cell thermodynamics and a new role for protein surfaces

G. Pielak, Austin E. Smith, Michael Senske, 2016, Proceedings of the National Academy of Sciences.

(19) F NMR spectroscopy as a probe of cytoplasmic viscosity and weak protein interactions in living cells.

Zeting Zhang, B. Jiang, Xu Zhang, 2013, Chemistry.

Protecting enzymes from stress-induced inactivation.

G. Pielak, Samantha Piszkiewicz, 2019, Biochemistry.

Magnetic Resonance Spectroscopy as a Tool for Assessing Macromolecular Structure and Function in Living Cells.

Zeting Zhang, Conggang Li, Maili Liu, 2017, Annual review of analytical chemistry.

In‐cell protein NMR and protein leakage

G. Pielak, C. Barnes, Gary J Pielak, 2011, Proteins.

Enthalpic stabilization of an SH3 domain by D2O

G. Pielak, Samantha S. Stadmiller, 2018, Protein science : a publication of the Protein Society.

Roles of structural plasticity in chaperone HdeA activity are revealed by 19 F NMR †

Conggang Li, Maili Liu, G. Pielak, 2015 .

Protein-complex stability in cells and in vitro under crowded conditions.

G. Pielak, Samantha S. Stadmiller, 2020, Current opinion in structural biology.

Searching for quantitative entropy‐enthalpy compensation among protein variants

G. Pielak, Lixin Chen, D. Doyle, 2002, Proteins.

Nonideality and protein thermal denaturation.

M. Edgell, G. Pielak, S. Lahr, 1999, Biopolymers.

Dramatic stabilization of ferricytochrome c upon reduction.

G. Pielak, E. F. Bowden, S. Hilgen-Willis, 1993, Journal of inorganic biochemistry.

Requirements for perpendicular helix pairing

G. Pielak, J. Beasley, 1996, Proteins.

Protein shape modulates crowding effects

G. Pielak, G. B. Young, Alex J. Guseman, 2018, Proceedings of the National Academy of Sciences.

Large cosolutes, small cosolutes, and dihydrofolate reductase activity

G. Pielak, Annelise H. Gorensek-Benitez, Gerardo M Perez Goncalves, 2017, Protein science : a publication of the Protein Society.

Soft interactions and crowding

Conggang Li, Mohona Sarkar, G. Pielak, 2013, Biophysical Reviews.

Disordered Protein Diffusion under Crowded Conditions.

G. Pielak, Yaqiang Wang, Laura A Benton, 2012, The journal of physical chemistry letters.

Volume exclusion and soft interaction effects on protein stability under crowded conditions.

Andrew C. Miklos, Conggang Li, Conggang Li, 2010, Biochemistry.

Effects of proteins on protein diffusion.

Conggang Li, Conggang Li, G. Pielak, 2010, Journal of the American Chemical Society.

Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix.

G J Pielak, G. Pielak, Z L Fredericks, 1993, Biochemistry.

Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis.

D. Auld, G. Pielak, 1991, Biochemistry.

Two-dimensional NMR as a probe of structural similarity applied to mutants of cytochrome c.

R. J. Williams, G. Pielak, R. Atkinson, 1988, European journal of biochemistry.

Unusual effects of an engineered disulfide on global and local protein stability.

S. Betz, G. Pielak, D. Doyle, 1996, Biochemistry.

A cell is more than the sum of its (dilute) parts: A brief history of quinary structure

G. Pielak, Rachel D. Cohen, 2017, Protein science : a publication of the Protein Society.

Impact of reconstituted cytosol on protein stability

Gary J. Pielak, Mohona Sarkar, G. Pielak, 2013, Proceedings of the National Academy of Sciences.

Secondary structure and stability of a gel‐forming tardigrade desiccation‐tolerance protein

G. Pielak, S. Sheiko, J. Atkin, 2022, Protein science : a publication of the Protein Society.

An osmolyte mitigates the destabilizing effect of protein crowding

Mohona Sarkar, G. Pielak, 2014, Protein science : a publication of the Protein Society.

Macromolecular Crowding Is More than Hard-Core Repulsions.

G. Pielak, D. Harries, Liel Sapir, 2022, Annual review of biophysics.

Protection by desiccation‐tolerance proteins probed at the residue level

G. Pielak, Owen Warmuth, Candice J. Crilly, 2021, Protein science : a publication of the Protein Society.

Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR.

G. Pielak, J. Atkin, Owen Warmuth, 2021, Biochemistry.

Intrinsically Disordered Proteins and Desiccation Tolerance: Elucidating Functional and Mechanistic Underpinnings of Anhydrobiosis

G. Pielak, Thomas C. Boothby, T. Boothby, 2017, BioEssays : news and reviews in molecular, cellular and developmental biology.

Stability of yeast iso‐1‐ferricytochrome c as a function of pH and temperature

G. Pielak, D. Cohen, 1994, Protein science : a publication of the Protein Society.

Electron-proton coupling in cytochrome c studied using protein variants.

R. J. Williams, G. Pielak, G. Mclendon, 1992, European journal of biochemistry.

How Sugars Protect Dry Protein Structure

G. Pielak, Julia A Brom, Ruta G Petrikis, 2023, Biochemistry.

Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.

G. Pielak, I. G. Zigoneanu, Rebecca A. S. Ruf, 2008, Biochemistry.

Quinary interactions with an unfolded state ensemble

G. Pielak, Rachel D. Cohen, 2017, Protein science : a publication of the Protein Society.

Electrostatic Contributions to Protein Quinary Structure.

G. Pielak, Rachel D. Cohen, 2016, Journal of the American Chemical Society.

Quinary structure modulates protein stability in cells

G. Pielak, Austin E. Smith, Rachel D. Cohen, 2015, Proceedings of the National Academy of Sciences.

Residue level quantification of protein stability in living cells

G. Pielak, W. Monteith, 2014, Proceedings of the National Academy of Sciences.

Protein crowder charge and protein stability.

Mohona Sarkar, G. Pielak, J. Lu, 2014, Biochemistry.

Changes in global stability and local structure of cytochrome c upon substituting phenylalanine-82 with tyrosine.

D. Auld, S. Betz, G. Pielak, 1993, Journal of inorganic biochemistry.

Amide proton exchange rates of oxidized and reduced saccharomyces cerevisiae iso‐1‐cytochrome c

D. Auld, S. Betz, G. Pielak, 1993, Protein science : a publication of the Protein Society.

Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants.

G J Pielak, G. Pielak, B. Hoffman, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Temperature-sensitive variants of Saccharomyces cerevisiae iso-1-cytochrome c produced by random mutagenesis of codons 43 to 54.

G. Pielak, X. Wang, 1991, Journal of molecular biology.

Quantifying green fluorescent protein diffusion in Escherichia coli by using continuous photobleaching with evanescent illumination.

N. Thompson, G. Pielak, B. L. Steele, 2009, The journal of physical chemistry. B.

Novel axial ligand interchange in cytochrome c: Incorporation of a histidine at position 82 leads to displacement of the wild-type methionine-80 ligand

G. Pielak, J. Dawson, B. Hawkins, 1994 .

Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase.

G. Pielak, B. Durham, F. Millett, 1999, Biochemistry.

19F NMR studies of α‐synuclein‐membrane interactions

Guifang Wang, Conggang Li, G. Pielak, 2010, Protein science : a publication of the Protein Society.

Intracellular pH modulates quinary structure

G. Pielak, Alex J. Guseman, Rachel D. Cohen, 2015, Protein science : a publication of the Protein Society.

Internal and Global Protein Motion Assessed with a Fusion Construct and In‐Cell NMR Spectroscopy

G. Pielak, C. Barnes, Gary J Pielak, 2011, Chembiochem : a European journal of chemical biology.

A bioreactor for in-cell protein NMR.

G. Pielak, N. G. Sharaf, C. Barnes, 2010, Journal of magnetic resonance.

Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes and under crowded conditions in vitro and in cells

G. Pielak, I. Chu, 2023, Magnetic Resonance Letters.

Resolving the enthalpy of protein stabilization by macromolecular crowding

G. Pielak, D. Harries, C. Stewart, 2023, Protein science : a publication of the Protein Society.

Cosolutes, Crowding, and Protein Folding Kinetics.

G. Pielak, Samantha S. Stadmiller, Austin E. Smith, 2017, The journal of physical chemistry. B.

Temperature‐induced reversible conformational change in the first 100 residues of α‐synuclein

G. Pielak, A. Tripathy, G. B. Young, 2006 .

Entropic Stabilization of Cytochrome c upon Reduction

Gary J. Pielak, G. Pielak, David S. Cohen, 1995 .

Polarity of disulfide bonds

G. Pielak, G. B. Young, A. Saunders, 1993, Protein science : a publication of the Protein Society.

A native tertiary interaction stabilizes the A state of cytochrome c.

G. Pielak, J. Marmorino, 1995, Biochemistry.

Macromolecular crowding and protein stability.

Mohona Sarkar, G. Pielak, Yaqiang Wang, 2012, Journal of the American Chemical Society.

Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions.

Conggang Li, G. Pielak, 2009, Journal of the American Chemical Society.

Quantifying GFP Diffusion in Escherichia coli by Using Continuous Photobleaching with Evanescent Illumination

N. Thompson, G. Pielak, B. L. Steele, 2009 .

Surface Charge Modulates Protein-Protein Interactions in Physiologically Relevant Environments.

G. Pielak, Alex J. Guseman, Shannon L. Speer, 2018, Biochemistry.

Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory.

G. Pielak, X. Wang, A. S. Morar, 2001, Biochemistry.

Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli.

N. Thompson, G. Pielak, R. Baker, 2009, Biochemistry.

Disordered proteins mitigate the temperature dependence of site-specific binding free energies

G. Pielak, C. Waudby, Joseph F. Thole, 2023, The Journal of biological chemistry.

Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy.

Jeffrey M. Macdonald, Guifang Wang, Gary J. Pielak, 2008, Journal of the American Chemical Society.

Trifluoroethanol and the behavior of a tardigrade desiccation‐tolerance protein

G. Pielak, S. Wang, Jonathan Eicher, 2023, Protein science : a publication of the Protein Society.

Effects of molecular crowding by saccharides on α‐chymotrypsin dimerization

Ashutosh Tripathy, D. Winzor, G. Pielak, 2002, Protein science : a publication of the Protein Society.

Peroxidative aggregation of α‐synuclein requires tyrosines

G. Pielak, A. Olteanu, 2004 .

The Cytoplasmic Region of Mouse FcγRIIb1, but Not FcγRIIb2, Binds Phospholipid Membranes†

N. Thompson, G. Pielak, Lixin Chen, 1999 .

Protein nuclear magnetic resonance under physiological conditions.

Andrew C. Miklos, Gui-Fang Wang, Conggang Li, 2009, Biochemistry.

Amide proton exchange of a dynamic loop in cell extracts

Mohona Sarkar, G. Pielak, G. B. Young, 2013, Protein science : a publication of the Protein Society.

Chapter 12. Protein Stability and Weak Intracellular Interactions

G. Pielak, Alex J. Guseman, 2019, New Developments in NMR.

Macromolecular Crowding by Polyethylene Glycol Reduces Protein Breathing.

Brent O Hutcheson, G. Pielak, I. Chu, 2023, The journal of physical chemistry letters.

Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure.

G J Pielak, C. Carter, M. Edgell, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Changing the transition state for protein (Un) folding.

S. Parikh, G. Pielak, D. Doyle, 1996, Biochemistry.

Residue level quantification of protein stability in living cells

G. Pielak, W. Monteith, 2014, Proceedings of the National Academy of Sciences.

Crowding and Confinement Can Oppositely Affect Protein Stability.

Zeting Zhang, Conggang Li, Maili Liu, 2018, Chemphyschem : a European journal of chemical physics and physical chemistry.

Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface.

D F Doyle, G J Pielak, G. Pielak, 1995, Biochemistry.

Probing weakly polar interactions in cytochrome c

D. Auld, S. Betz, G. Pielak, 1993, Protein science : a publication of the Protein Society.

Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability.

Andrew C. Miklos, Conggang Li, G. Pielak, 2009, Methods in enzymology.

Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.

G. Pielak, Gil I Olgenblum, Daniel Harries, 2024, Chemical reviews.

1H and 15N Hyperfine Shifts of Cytochrome c

C. Dobson, G. Pielak, J. Boyd, 1999 .

Macromolecular crowding fails to fold a globular protein in cells.

G. Pielak, Yaqiang Wang, Alexander P. Schlesinger, 2011, Journal of the American Chemical Society.

Osmolytes and Protein-Protein Interactions.

E. Brustad, G. Pielak, Amy E Rydeen, 2018, Journal of the American Chemical Society.