Skip to main content
The Pielak Group
Group Publications
Brom JA, Samsri S, Petrikis, RG, Parnham S, Pielak GJ. 2023. 1H, 13C, 15N backbone resonance assignment of Escherichia coli adenylate kinase. Biomolecular NMR assignments. 17: 235-238.
Wang S, Eicher JE, Pielak GJ. 2023. Trifluoroethanol and the behavior of a tardigrade desiccation-tolerance protein. Protein Science, 32: e4716.
Eicher JE, Hutcheson BO, Pielak GJ. 2023. Properties of a tardigrade desiccation-tolerance protein aerogel. Biophysical Journal, 122: 2500-2505.
Chu IT, Pielak GJ. 2023. Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in colsolutes, under crowded conditions in vitro and in cells. Magnetic Resonance Letters 3: 319-326.
Chu I-T, Hutcheson BO, Malsch HR, Pielak GJ. 2023. Macromolecular crowding by polyethylene glycol reduces protein breathing. Journal of Physical Chemistry Letters, 14: 2599-2605.
Brom JA., Petrikis RG, Pielak GJ. 2023. How sugars protect dry protein structure. Biochemistry, 62: 1044-1052.
Thole JF, Waudby C, Pielak GJ. 2023. Disordered proteins mitigate the temperature dependence of site-specific binding free energies Journal of Biological Chemistry, 299: 102984.
Stewart CJ, Olgenblum GI, Propst A, Harries D, Pielak GJ. 2023. Resolving the enthalpy of protein stabilization by macromolecular crowding Protein Science, 31: e4573.
Eicher JE, Brom JA, Wang S, Sheiko SS, Atkin JM, Pielak GJ. 2022. Secondary structure and stability of a gel-forming tardigrade desiccation-tolerance protein. Protein Science,31, e4495.
Zhang C, Pei Y, Zhang Z, Xu L, Liu X, Jiang L, Pielak GJ, Zhou X, Liu M, Li C. 2022. C-terminal truncation modulates α-synuclein’s cytotoxicity and aggregation by promoting the interactions with membrane and chaperone. Communications Biology, 5: 798.
Brom J, Pielak GJ. 2022. Desiccation-tolerance- and globular- proteins adsorb similar amounts of water. Protein Science, 31: e4288.
Chu I-T, Stewart CJ, Speer SL, Pielak GJ. 2022. A difference between in vitro and in-cell protein dimer formation. Biochemistry, 61: 409-412..
Speer SL, Stewart C, Sapir L, Harries D, Pielak GJ. 2022. Macromolecular crowding is more than hard-core repulsions. Annual Review of Biophysics, 51: 267-300.
Crilly C, Brom JA, Warmuth O, Esterly HJ. 2022. Protection by desiccation-tolerance proteins probed at the residue level. Protein Science, 31: 396-406.
Crilly C, Eicher JE, Warmuth O, Atkin JM, Pielak GJ. 2021. Water’s variable role in protein stability uncovered by liquid-observed vapor exchange NMR. Biochemistry, 60: 3041–3045.
Pielak GJ. 2021. Buffers, especially the good kind. Biochemistry, 60: 3436-3440.
Gruebele M, Pielak GJ. 2021. Dynamical spectroscopy and microscopy of proteins in cells. Current Opinion in Structural Biology, 70: 1-7.
Speer SL, Zheng W, Jiang X, Chu I-T, Guseman AJ, Liu M, Pielak GJ, Li C. 2021. The intracellular environment affects protein-protein interactions. Proceedings of the National Academy of Sciences of the United States of America, 118: e2019918118.
Thole J, Fadero T, Bonin J, Stadmiller S, Giudice J, Pielak G. 2021. Danio rerio oocytes for eukaryotic in-cell NMR. Biochemistry, 60: 451-459.
Crilly C, Brom J, Kowalewski ME, Piszkiewicz S, Pielak, GJ. 2021. Dried protein structure revealed at the residue level by liquid-observed vapor exchange NMR. Biochemistry 60: 152-159.

Stadmiller SS, Pielak GJ. 2020. Protein-complex stability in cells and in vitro under crowded conditions. Current Opinions in Structural Biology 66: 183-192 press.

Stadmiller SS, Aguilar JS, Parnham S, Pielak GJ. 2020. Protein-peptide binding energetics under crowded conditions. Journal of Physical Chemistry, 124: 9297-9309.

Esterly HJ, Crilly C, Piszkiewicz S, Shovlin DJ, Pielak GJ, Christian BE. 2020. Toxicity and immunogenicity of a tardigrade cytosolic abundant heat soluble protein in mice. Frontiers in Pharmacology, 11: 1571.

Stadmiller SS, Aguilar, JS, Waudby C, Pielak GJ. 2020. Rapid quantification of protein-ligand binding via 19F NMR lineshape analysis. Biophysical Journal, 118: 2337-2348.

Chu I-T, Speer SL, Pielak GJ. 2020. Rheostatic control of protein expression using Tuner cells. Biochemistry, 59: 733-735.

Guseman AJ, Pielak GJ (2020). Chapter 12. Protein stability and weak intracellular interactions. In-cell NMR spectroscopy: From molecular sciences to cell biology, eds Ito Y, Dötsch V, & Shirakawa M (The Royal Society of Chemistry), pp 188-206.

Pielak G, Piszkiewicz S 2019. Protecting enzymes from stress-induced inactivation Biochemistry 58: 3825-3833.

Speer SL, Guseman AJ, Patteson JB, Ehrmann BM, & Pielak GJ (2019) Controlling and quantifying protein concentration in Escherichia coli. Protein Science, 28: 1307-131.

Ye Y, Wu Q, Zheng W, Jiang B, Pielak G, Liu M, Li C. 2019. Positively-charged tags impede protein mobility in cells as quantified by 19F NMR. Journal of Physical Chemistry, 123: 4527-4533.

Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. 2019. Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and snare-complex assembly. The FASEB Journal, 33: 7985-7994.

Piszkiewicz S, Gunn KH, Warmuth O, Propst A, Mehta A, Nguyen KH, Kuhlman E, Guseman AJ, Stadmiller SS, Boothby TC, Neher SB, & Pielak GJ. 2019. Protecting activity of desiccated enzymes. Protein Science, 28: 941-951.

Carter C, Wolfenden R, Caplow M, Lentz B, Pielak G, Watenpaugh K, Hu H, Puett D. 2019. Jan Hermans (1933-2018): Red-blooded biophysicists study hemoglobin. Proteins, 87:171-173.

Cheng K, Wu Q, Zhang Z, Pielak GJ, Liu M, Li C. 2018. Crowding and confinement can oppositely affect protein stability. ChemPhysChem, 19: 1-7.

Guseman AJ, Perez Goncalves GM, Speer SL, Young GB, Pielak GH. 2018. Protein shape modulates crowding effects. Proceedings of the National Academy of Sciences of the United States of America, 115: 10965-10970.

Stadmiller SS, Pielak GJ. 2018 Enthalpic stabilization of an SH3 domain D2O. Protein Science, 27: 1710-1716.

Rydeen AE, Brustad EM, Pielak GJ. 2018. Osmolytes and protein-protein interactions. Journal of the American Chemical Society. 140: 7441-7444.

Guseman AJ, Speer SL, Perez Goncalves GM, Pielak GJ. 2018. Surface charge modulates protein-protein interactions in physiologically relevant environments. Biochemistry, 57: 1681-1684.

Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C. 2017. Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy. Analytical and Bioanalytical Chemistry, 410: 869-874.

Acosta LC, Perez Goncalves GM, Pielak GJ, Gorensek-Benitez AH. 2017. Large cosolutes, small cosolutes and dihydrofolate reductase activity. Protein Science, 26: 2417-2425.

Boothby, TC, Pielak GJ. 2017. Intrinsically disordered proteins and desiccation tolerance: elucidating functional and mechanistic underpinnings of anhydrobiosis. BioEssays, 39 (11).

Gorensek-Benitez AH, Smith AE, Stadmiller SS, Perez Goncalves GM, Pielak GJ. 2017. Cosolutes, crowding, and protein folding kinetics. Journal of Physical Chemistry B, 121: 6527-6537.

Cohen RD, Pielak GJ. 2017. Quinary interactions with an unfolded state ensemble. Protein Science, 26: 1698-1703.

Li C, Zhao J, Cheng K, Ge Y, Wu Q, Ye Y, Xu G, Zhang Z, Zhang X, Zhou X, Pielak GJ, Liu M. 2017. Magnetic resonance spectroscopy as a tool for assessing macromolecular structure and function in living cells. Annual Review of Analytical Chemistry,10: 157-182.

Stadmiller S.S. Gorensek-Benitez AH, Guseman AJ, Pielak GJ. 2017. Osmotic-shock induced protein destabilization in living cells and its reversal by glycine betaine. Journal of Molecular Biology, 429: 1155–1161.

Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, & Goldstein B. 2017. Tardigrades use intrinsically disordered proteins to survive desiccation. Molecular Cell, 65: 975–984.

Guseman, AJ, Pielak GJ. 2017. Cosolute and Crowding Effects on a Side-By-Side Protein Dimer. Biochemistry, 56: 971-976.

Cohen RD, Pielak GJ. 2016. A cell is more than the sum of its (dilute) parts: a brief history of quinary structure. Protein Science, 26: 403-413.

Bia J, Pielak GJ, Li C. 2016. Macromolecular and small molecule crowding have similar effects on α-synuclein structure. ChemPhysChem, 18, 55-58.

Cohen RD, Pielak GJ. 2016. Electostatic contribution to protein quinary structure. Journal of the American Chemical Society, 138: 13139–13142.

Senske M, Smith AE, Pielak GJ. 2016. Protein stability in reverse micelles. Angewandte Chemie, 55: 3586-3589.

Smith AE, Zhou LZ, Gorensek AH, Senske M, Pielak GJ. 2016. In-cell thermodynamics and a new role for protein surfaces. Proceedings of the National Academy of Sciences of the United States of America, 113: 1725-1730. Commentary in PNAS. Featured by Faculty of 1000.

Zhaia Z, Wua Q, Zheng W, Liu M, Pielak GJ, Li C. 2016. Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR. Chemical Science, 7, 2222-2228.

Tyrrell J, Weeks, KM, Pielak GJ. 2015. Challenge of mimicking the influences of the cellular environment on RNA structure by PEG-induced macromolecular crowding. Biochemistry, 54: 6447-6453. Featured by Faculty of 1000.

Cohen RD, Guseman AJ, Pielak GJ. 2015. Intracellular pH modulates quinary structure. Protein Science, 24: 1748-1755.

Spitzer J, Pielak GJ, Poolman B. 2015. Emergence of life: Physical chemistry changes the paradigm. Biology Direct, 10: 33.

Smith AE, Zhou Z, Pielak GJ. 2015. Hydrogen exchange of disordered proteins in Escherichia coli. Protein Science. 24: 706-713.

Monteith WB, Cohen RD, Smith AE, Guzman-Cisneros E, Pielak, GJ. 2015. Quinary structure modulates protein stability in cells. Proceedings of the National Academy of Sciences of the United States of America, 112: 1739-1742.

Smith AE, Zhang Z, Pielak GJ, Li C 2015. NMR studicells and cell-like environments. Current Opinion in Structural Biology: 30: 7-16.

Sarkar M, Pielak GJ. 2014. An osmolyte mitigates the destabilizing effect of protein crowding. Protein Science 23: 1161-1164. Cover article.

Monteith WB, Pielak GJ. 2014. Residue level quantification of protein stability in living cells. Proceedings of the National Academy of Sciences of the United States of Americal: 111: 11335-11340. Featured by Faculty of 1000. Correction.

Theillet F-X, Binolfi A, Frembgen-Kesner T, Hingorani K, Sarkar M, Kyne C, Li C, Crowley P, Gierasch L, Pielak G, Elcock A, Gershenson A, Selenko P. 2014. Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chemical Reviews 114: 6661-6714.

Sarkar M, Lu J, Pielak GJ. 2014. Protein-crowder charge and protein stability. Biochemistry 53:1601-1606.

Xu G, Ye Y, Liu X, Cao S, Wu Q, Cheng K, Liu M, Pielak GJ, Li C. 2014. Strategies for protein NMR in Escherichia coli. Biochemistry 53: 1971-1981.

Sarkar M, Smith AE, Pielak GJ. 2013. Impact of reconstituted cytosol on protein stability. Proceeding of the National Academy of Sciences of the United Sates of America 110:19342-19347. Featured by Faculty of 1000.

Smith A, Sarkar M, Young G, Pielak GJ. 2013. Amide proton exchange of a dynamic loop in cell extracts. Protein Science 22:1313-1319.

Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, Jiang L, Zhang X, Liu M, Pielak GJ, C Li C. 2013. 19F NMR as a probe of cytoplasmic viscosity and weak protein interactions in living cells. Chemistry--A European Journal 19: 12705-12710.

Sarkar M, Li C, Pielak GJ. 2013. Soft interactions and crowding. Biophysical Reviews 5: 187-194.

Tyrrell J, McGinnis JL, Weeks KM, & Pielak GJ (2013) The cellular environment stabilizes adenine riboswitch RNA structure. Biochemistry 52: 8777–8785. Featured by Faculty of 1000.

Benton LA, Smith AE, Young GB, Pielak GJ. 2012. Unexpected effects of macromolecular crowding on protein stability. Biochemistry 51: 9773-9775.

Wang Y, Sarkar M, Smith AE, Krois AS, Pielak GJ. 2012.Macromolecular crowding and protein stability. Journal of the American Chemical Society 134: 16614-16618.

Wang Y, Benton L, Singh V, Pielak GJ. 2012. Disordered protein diffusion under crowded conditions. Journal of Physical Chemistry Letters 3: 2703- 2706.

Wang Y, Li C, Pielak GJ. 2012. In-cell protein magnetic resonance spectroscopy. Chinese Journal of Magnetic Resonance 29: 475-488.

Pielak GJ, Tian F. 2012. Membrane proteins, magic-angle spinning, and in-cell NMR. Proceedings of the National Academy of Sciences of the United States of America 109: 4715-4716.

Zigoneanu IG, Pielak GJ 2012. Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by 19F NMR. Molecular Pharmaceutics 9: 1024-1029.

Zigoneanu IG, Yang YJ, Krois AS, Haque Md E, Pielak GJ. 2012. Interaction of α-synuclein and its A30P variant with vesicles of composition similar to mitochondrial membranes. Biochimica Biophysica Acta 1818: 512-519.

Fu R, Wang X, Li C, Santiago-Miranda A, Pielak GJ, Tian F. 2011. In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state MAS NMR. Journal of the American Chemical Society 133: 12370-12373.

Schlesinger AP, Wang Y, Tadeo X, Millet O, Pielak GJ. 2011. Macromolecular crowding fails to fold a globular protein in cells. Journal of the American Chemical Society 133: 8082-8085.

Miklos AC, Sarkar M, Wang Y, Pielak GJ. 2011. Proteins crowding tunes protein stability. Journal of the American Chemical Society 133: 7116-7120. Featured by Faculty of 1000.

Miklos AC, Li C, Sorrell CD, Lyon LA, Pielak GJ. 2011. An upper limit for macromolecular crowding effects. BMC Biophysics, 4: 13.

Barnes CO, Monteith WB, Pielak GJ. 2011. Internal and global protein motion assessed with a fusion construct and in-cell NMR. ChemBiochem 12: 390-391.

Barnes CO, Pielak GJ. 2011. In-cell protein NMR and protein leakage. Proteins: Structure, Function, and Bioinformatics 79: 347-351.

Miklos AC, Pielak GJ. 2010. Crowding and function reunite. Proceedings of the National Academy of Sciences of the United States of America 107: 17457-17458.

Wang, G-F, Li C, Pielak GJ. 2010. Probing the micelle-bound aggregation-prone state of α-synuclein with 19F NMR. ChemBioChem 11: 1993-1996.

Miklos AC, Li C, Sharaf NG, Pielak GJ. 2010. Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry 49: 6984-6991.

Wang G-F, Li C, Pielak GJ. 2010. 19F NMR studies of α-synuclein-membrane interactions. Protein Science 19: 1686-1691.

Wang Y, Li C, Pielak GJ. 2010. Effects of proteins on protein diffusion. Journal of the American Chemical Society 132: 9392-9397.

Li C, Wang G-F, Wang Y, Creager-Allen R, Lutz E A, Scronce,H, Slade K M. Ruf RA, Mehl RA Pielak GJ. 2010. Protein 19 NMR in Escherichia coli Journal of the American Chemical Society 132: 321-327. Featured in C&EN Concentrates.

Sharaf NG, Barnes CO, Charlton LM, Young GB, Pielak GJ. 2010. A bioreactor for in-cell protein NMR. Journal of Magnetic Resonance 202: 140-146. Cover article.

Miklos AC, Li C, Pielak GJ. 2009. Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability. Methods in Enzymology 466: 1-18.

Li C, Wang Y, Pielak GJ. 2009. Translational and rotational diffusion of a small globular protein under crowded conditions. Journal of Physical Chemistry B 113: 13390-13392.

Li C, Lutz EA, Slade KM, Ruf RA, Wang G, Pielak GJ. 2009. 19F-NMR studies of α-synuclein conformation and fibrillation. Biochemistry 48: 8578-8584.

Slade KM, Baker R, Chua M, Thompson NL, Pielak GJ. 2009. Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli. Biochemistry 48: 5083- 5089.

Slade KM, Steele BL, Pielak GJ, Thompson NL. 2009. Quantifying GFP diffusion in Escherichia coli by using continuous photobleaching with evanescent illumination. Journal of Physical Chemistry B 113: 4837-4845.

Li C, Pielak G J 2009. Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions, Journal of the American Chemical Society 131: 1368-1369

Pielak GJ, Li C, Miklos AC, Schlesinger AP, Slade, K M, Wang G., Zigoneanu IG. 2009. Protein NMR under physiological conditions, Biochemistry 48: 226-234.

Ruf RA, Lutz EA, Zigoneanu IG, Pielak G J. 2008. α-Synuclein conformation affects its tyrosine-dependant oxidative aggregation. Biochemistry 47: 13604-13609.

Li C, Charlton LM, Lakkavaram A, Seagle C, Wang G, Young GB, Macdonald JM, Pielak GJ. 2008. Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR. Journal of the American Chemical Society 130: 6310-6311.

Charlton LM, Barnes CO, Li C, Orans J, Young GB, Pielak GJ. 2008. Residue-level interrogation of macromolecular crowding effects on protein stability. Journal of the American Chemical Society 130: 6826-6830.

Pielak GJ, Patel CN, Winzor DJ. 2007. Reconsideration of sedimentation equilibrium distributions reflecting the effects of small inert cosolutes on the dimerization of α-chymotrypsin. Biophysical Chemistry 130: 89-92.

Charlton LM, Pielak GJ. 2006. Peeking into living eukaryotic cells with high-resolution NMR, Proceedings of the National Academy of Sciences of the United States of America 103: 11817-11818.

Bryant JE, Lecomte JTJ, Lee AL, Young GB, Pielak GJ. 2006. Cytosol has a small effect on protein backbone dynamics, Biochemistry 45: 10085-10091. Retracted: ibid. 2007. Biochemistry 46: 8206.

McCall S J, Nassar R, Malouf NN, Saunders AJ, Oakeley AE, Henderson PM, Solaro RJ, Pielak GJ, Alexander KA, and Anderson PAW. 2006. Development and cardiac contractility: cardiac troponin T isoforms and cytosolic calcium. Pediatric Research 60: 276-281.

Pielak GJ. 2006. Woes of proline: a cautionary kinetic tale. Protein
Science 15: 393-394.

McNulty BC, Young GB, Pielak GJ. 2006. Macromolecular crowding in the Escherichia coli periplasm maintains α-synuclein disorder. Journal of Molecular Biology 355: 893-897.

McNulty BC, Tripathy A, Young GB, Orans J, Pielak GJ 2006. Temperature-induced reversible conformational change in the first 100 residues of α-synuclein. Protein Science 15: 602-608.

Barrett DG, Minder CM, Mian MU, Whittington SJ, Cooper J, Fuchs KM, Tripathy A, Waters ML, Creamer TP, Pielak GJ. 2005. Pressure perturbation calorimetry of helical peptides. Proteins: Structure Function and Bioinformatics 63: 322-326.

Bryant JE, Lecomte JT, Lee AL, Young GB, Pielak GJ. 2005. Protein dynamics in living cells. Biochemistry 44: 9275 - 9279. Retracted: ibid. 2007. Biochemistry 46: 8206.

Pielak GJ. 2005. A model of cellular organization. Proceedings of the National Academy of Sciences of the United States of America 102: 5901-5902.

Yi F, Sims D, Pielak GJ, Edgell MH. 2005. Impact of robotics and instrument automation on protein stability measurements. Journal of the Association for Laboratory Automation 10: 98-101.

Olteanu A, Pielak GJ 2004. Peroxidative aggregation of α-synuclein requires tyrosines. Protein Science 13: 2852-2856.

Daughghdrill GW, Pielak GJ, Uversky VN, Cortese MS, Dunker AK. 2005. Natively Disordered Proteins. In Handbook of Protein Folding, ed. J Buchner, T Kiefhaber. Weinheim: Wiley-VCH, pp. 275-357.

Batchelor J D, Olteanu A, Tripathy A, Pielak GJ. 2004. Impact of protein denaturants and stabilizers on water structure. Journal of the American Chemical Society 126: 1958-1961.

Olteanu A, Patel CN, Dedmon MM, Kennedy S, Linhoff MW, Minder CM, Potts PR, Deshmukh M, Pielak GJ (2003). Stability and apoptotic activity of recombinant human cytochrome c. Biochemical and Biophysical Research Communications 312/3: 733-740.

Yi F, Sims DA, Pielak GJ, Edgell MH 2003. Testing hypotheses about determinants of protein structure with high-precision, high-throughput stability measurements and statistical modeling. Biochemistry 42: 7594-7603.

Edgell MH, Sims DA, Pielak GJ, Yi F 2003. High-precision, high-throughput stability determinations facilitated by robotics and a semi-automated titrating fluorometer. Biochemistry42: 7587-7593.

Engstrom G, Rajagukguk R, Saunders AJ, Patel CN, Rajagukguk S, Merbitz-Zahradnik T, Xiao K, Pielak GJ, Trumpower B, Yu C-A, Yu L, Durham B, Millett F 2003. Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry 42: 2816-2824.

Dedmon MM, Patel CN, Young GB, Pielak GJ. 2002. FlgM gains structure in living cells. Proceedings of the National Academy of Sciences of the United States of America 99: 12861-12864. Featured by Faculty of 1000.

Beasley JR, Doyle DF, Chen L, Cohen DS, Fine BR, Pielak GJ. 2002. Searching for quantitative entropy-enthalpy compensation among protein variants. Proteins: Structure, Function, and Genetics 49: 398-402.

Patel CN, Noble S., Weatherly GT, Tripathy A, Winzor DJ, Pielak GJ. 2002. Effects of molecular crowding by saccharides on alpha-chymotrypsin dimerization. Protein Science 11: 997-1003.

Morar AS, Pielak GJ. 2002. Crowding by trisaccharides and the 2:1 cytochrome c/cytochrome c peroxidase complex. Biochemistry 41: 547-551.

Morar AS, Olteanu A, Young GB, Pielak GJ. 2001. Solvent-induced collapse of alpha-synuclein and acid denatured cytochrome c. Protein Science 10: 195-199.

Patel C, Lind M, Pielak GJ. 2001. Characterization of horse cytochrome c expressed in Escherichia coli. Protein Expression and Purification 22: 220-224.

Davis-Searles PR, Saunders AJ, Erie DA, Winzor DJ, Pielak GJ. 2001. Interpreting the effects of small uncharged solutes on protein-folding equilibria. Annual Review of Biophysics and Bioengineering 30: 271-306.

Morar AS, Wang X, Pielak GJ. 2001. Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c / cytochrome c peroxidase binding: comparing theory to experiment. Biochemistry 40: 281-285.

Pielak GJ, Wang X. 2001. Interactions between yeast iso-1-cytochrome c and its peroxidase. Biochemistry 40: 422-428.

Weatherly GT, Pielak GJ. 2001. Second virial coefficients as a measure of protein-osmolyte interactions. Protein Science 10: 12-16.

Saunders AJ, Davis-Searles PR, Allen DL, Pielak GJ, Erie DA. 2000. Osmolyte-induced changes in protein conformational equilibria. Biopolymers 53: 293-307.

Boyd J, Dobson CM, Morar AS, Williams RJP, Pielak GJ. 1999. 1H and 15N hyperfine shifts of cytochrome c. Journal of the American Chemical Society121: 9247-9248.

Chen L, Pielak GJ, Thompson NL. 1999. The cytoplasmic region of Fc(g)RIIb1, but not Fc( g)RIIb2, binds phospholipids membranes. Biochemistry 38: 2102-2109.

Hostetter DR, Weatherly GT, Beasley JR, Bortone K, Cohen DS, Finger SA, Hardwidge P, Kakouras D, Saunders AJ, Trojak SK, Waldner JL, Pielak GJ. 1999. Partially formed native tertiary interactions in the A-state of cytochrome c. Journal of Molecular Biology 289: 639-644.

Lahr SJ, Broadwater A, Carter CW Jr., Collier ML, Hensley L, Waldner JL, Pielak GJ, Edgell MH. 1999. Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure. Proceedings of the National Academy of Sciences of the United States of America 96: 14860-14865.

Mei H, Wang K, Peffer N, Weatherly GT, Cohen DS, Pielak GJ, Durham B, Millett F. 1999. Role of configurational gating in intramolecular electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase. Biochemistry 39: 6846-6854.

Morar AS, Kakouras D, Young GB, Boyd J, Pielak GJ. 1999. Expression of 15 N-labeled eukaryotic cytochrome c in Escherichia coli. Journal of Biological Inorganic Chemistry 4: 220-222.

Waldner JL, Lahr SJ, Edgell MH, Pielak GJ. 1999. Nonideality and protein thermal denaturation. Biopolymers 49: 471-479.

Wang X, Pielak GJ. 1999. Equilibrium thermodynamics of a physiologically-relevant heme-protein complex. Biochemistry 38: 16876-16881.

Allen DL, Pielak GJ. 1998. Baseline length and automated fitting of denaturation data. Protein Science 7: 1262-1263.

Davis-Searles PR, Morar AS, Saunders AJ, Erie DA, Pielak GJ. 1998. Sugar-induced molten-globule model. Biochemistry: 17048-17053.

Fairris JL, Wang K, Geren L, Pielak GJ, Durham B, Millett F. 1998. Intramolecular electron transfer in yeast cytochrome c covalently bonded to ruthenium(II) polypyridine complexes at cys39. In: Photochemistry and Radiation Chemistry: American Chemical Society Advances in Chemistry Series 254. American Chemical Society: Washington, D.C. pp. 99-110.

Marmorino JL, Lehti M, Pielak GJ. 1998. Native tertiary structure in an A-state. Journal of Molecular Biology 275: 379-388.

Waldner JL, Lahr SJ, Edgell MH Pielak GJ. 1998. Effects of a polyhistidine terminal extension on eglin c stability. Analytical Biochemistry 263: 116-118.

Wrobel JA, Chao S-F, Conrad MJ, Merker JD, Swanstrom R, Pielak GJ, Hutchison, CA, III. 1998. A genetic approach for identifying critical residues in the fingers and palm subdomains of HIV-1 reverse transcriptase. Proceedings of the National Academy of Sciences of the United States of America 95: 638-645.

Chen L, Thompson NL, Pielak GJ. 1997. Design, synthesis, and characterization of the genes for mouse Fc g RIIb1 and Fc g RIIb2 cytoplasmic regions. Protein Science 6: 1038-1046.

Pielak GJ. 1997. Review of "Circular dichroism and the conformational analysis of biomolecules." Fasman, G.D., Ed., Plenum, NY (1997). American Scientist 85: 391-392.

Beasley JR, Pielak GJ. 1996. Requirements for perpendicular helix pairing. Proteins: Structure Function And Genetics 26: 95-107.

Betz SF, Marmorino JL, Saunders AJ, Doyle DF, Young GB Pielak GJ. 1996. Unusual effects of an engineered disulfide on global and local protein stability. Biochemistry 35: 7422-7428.

Doyle DF, Waldner JL, Parikh S, Alcazar-Roman L, Pielak GJ. 1996. Changing the transition state for protein (un)folding. Biochemistry 35: 7403-7411.

Mei H, Wang K, McKee S, Wang X, Waldner JL, Pielak GJ, Durham B, Millett F. 1996. 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. Biochemistry 35: 15800-15806.

Miller MA, Geren L, Han GW, Saunders A, Beasley J, Pielak GJ, Durham B, Millett F, Kraut J. 1996. Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering. Biochemistry 35: 667-673.

Pappa HS, Tajbaksh S, Saunders AJ, Pielak GJ, Poulos TL. 1996. Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific crosslinking. Biochemistry 35: 4837-4845.

Pielak GJ, Auld DS, Betz SF, Hilgen-Willis SE, Garcia LL. 1996. Nuclear magnetic resonance studies of class I cytochromes c. In: Scott RA, Mauk AG, eds. Cytochromes c: A Multidisciplinary Approach. Sausalito: University Science Books. pp. 203-284.

Wang K, Mei H, Geren L, Miller MA, Saunders A, Wang X, Waldner JL, Pielak GJ, Durham B, Millett F. 1996. Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase. Biochemistry 35: 15107-15119.

Cohen DS, Pielak GJ. 1995. Entropic stabilization of cytochrome c upon reduction. Journal of the American Chemical Society 117: 1675-1677.

Geren LM, Beasley JR, Fine BR, Saunders AJ, Hibdon S, Pielak GJ, Durham B, Millett F. 1995. Design of a ruthenium-cytochrome c derivative to measure electron transfer to the initial acceptor in cytochrome c oxidase. Journal of Biological Chemistry 270: 2466-2472.

Marmorino JL, Pielak GJ. 1995. A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry 34: 3140-3143.

Pielak GJ, Auld DS, Beasley JR, Betz SF, Cohen DS, Doyle DF, Finger SA, Fredericks ZL, Hilgen-Willis S, Saunders AJ, Trojak SK. 1995. Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface. Biochemistry 34: 3268-3276.

Cohen DS, Pielak GJ. 1994. The stability of yeast iso-1-cytochrome c as a function of pH and temperature. Protein Science 3: 1253-1260.

Auld DS, Young GB, Saunders AJ, Doyle DF, Pielak GJ. 1993. Probing weakly-polar interactions in cytochrome c. Protein Science 2: 2187-2197.

Fredericks ZL, Pielak GJ. 1993. Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix. Biochemistry 32: 929-936.

Hilgen-Willis S, Bowden EF, Pielak GJ. 1993. Dramatic stabilization of ferricytochrome c upon reduction. Journal of Inorganic Biochemistry 51: 649-653.

Marmorino,JL, Auld DS, Betz SF, Doyle DF, Young GB, Pielak GJ. 1993. Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c. Protein Science 2: 1966-1974.

Saunders AJ, Young GB, Pielak GJ. 1993. Polarity of disulfide bonds. Protein Science 2: 1183-1184.

Greene RM, Betz SF, Hilgen-Willis S, Auld DS, Fencl JB, Pielak GJ. 1993. Changes in global stability and local structure of cytochrome c upon substituting phenylalanine-82 with tyrosine. Journal of Inorganic Biochemistry 51: 663-676.

Willie A, McLean M, Liu R-Q, Hilgen-Willis S, Saunders AJ, Pielak GJ, Sligar SG, Durham B, Millett F. 1993. Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c. Biochemistry32: 7519-7525. Betz SF, Pielak GJ. 1992. Introduction of a disulfide bind into cytochrome c stabilizes a compact denatured state. Biochemistry 31: 12337-12344.

Gao Y, McLendon G, Pielak GJ, Williams RJP. 1992. Electron-proton coupling in cytochrome c studied using protein variants. European Journal of Biochemistry204: 337-352.

Auld DS, Pielak GJ. 1991. Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis. Biochemistry 30: 8684-8690.

Concar DW, Whitford, D, Pielak GJ, Williams RJP. 1991. The role of phenylalanine-82 in electron-exchange reactions of eukaryotic cytochromes c. Journal of the American Chemical Society 113: 2401-2406.

Gao Y, Boyd J, Pielak GJ, Williams RJP. 1991. 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. Biochemistry 30: 7033-7040.

Gao Y, Boyd J, Pielak GJ, Williams RJP. 1991. Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts. Biochemistry 30: 1928-1934.

Hilgen SE, Pielak GJ. 1991. The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue phe82 when the gene is present on a low copy number vector. Protein Engineering 4: 575-578.

Thurgood AGP, Pielak GJ, Cutler RL, Davies AM, Greenwood C, Mauk AG, Smith M, Williamson DJ, Moore, GR. 1991. Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. Federation of European Biochemical Societies Letters 284: 173-177.

Wang X, Pielak GJ. 1991. Temperature-sensitive variants of Saccharomyces cerevisiae iso-1- cytochrome c produced by random mutagenesis of codons 43 to 54. Journal of Molecular Biology 221: 97-105.

Hildebrandt P, Pielak GJ, Williams RJP. 1991. Structural studies of yeast iso-1-cytochrome c mutants by resonance Raman spectroscopy. European Journal of Biochemistry 201: 211-216.

Gao Y, Boyd J, Williams RJ, Pielak GJ. 1990. 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. Biochemistry 29: 6994-7003.

Liang N, Mauk AG, Pielak GJ, Johnson JA, Smith M, Hoffman BM. 1988. Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science 240: 311-313.

Pielak GJ, Atkinson RA, Boyd J, Williams RJP. 1988. Two-dimensional NMR as a probe of structural similarity applied to mutants of cytochrome c. European Journal of Biochemistry177: 179-185.

Pielak GJ, Boyd J, Moore GR, Williams RJP. 1988. Proton NMR studies show that the THR 102 mutant of yeast iso-1-cytochrome c is a typical member of the cytochrome c family. European Journal of Biochemistry 177: 167-177.

Cutler RL, Pielak GJ, Mauk AG, Smith M. 1987. Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1- cytochrome c with threonine: improved stability of the mutant protein. Protein Engineering 1: 95-99.

Liang N, Pielak GJ, Mauk AG, Smith M, Hoffman BM. 1987. 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 serine-87 or glycine-87 variants. Proceedings of the National Academy of Sciences of the United States of America 84: 1249-1252.

Pielak GJ, Concar DW, Moore GR, Williams RJP. 1987. The structure of cytochrome c and its relation to recent studies of long-range electron transfer. Protein Engineering 1: 83-88.

Pielak GJ, Oikawa K, Mauk AG, Smith M, Kay CM. 1986. Elimination of the negative Soret Cotton effect of eukaryotic cytochromes c by replacement of an invariant phenylalanine residue by site-directed mutagenesis. Journal of the American Chemical Society 108: 2724-2727.

Pielak GJ, Gurusiddiwiah S, Legg JI. 1986. Quantification of azo-coupled lysine in azo proteins by amino acid analysis. Analytical Biochemistry 56: 403-405.

Pielak GJ, Mauk AG, Smith M. 1985. Site-directed mutagenesis of cytochrome c shows that an invariant phe is not essential for function. Nature 313: 152-154.

Pielak GJ, Urdea MS, Legg JI. 1984. Preparation and characterization of arsanilazo and sulfanilazo proteins. Biochemistry 23: 596-603.

Pielak GJ, Urdea MS, Igi K, Legg JI. 1984. Azo protein analogs: synthesis and characterization of arsanilazo and sulfanilazo derivatives of tyrosine and histidine. Biochemistry 23: 589-596.

Legg JI, Igi K, Pielak GJ, Warner BD, Urdea MS. 1980. Circular dichroism as a probe of metal Ion interactions with azo proteins. In: Douglas BE, Yoshihiko S, eds. Stereochemistry of Optically Active Transition Metal Compounds. Washington, D.C.: American Chemical Society. pp. 195-205.