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C. Nick Pace - Publications

Affiliations: 
1968- Texas A & M College of Medicine, Bryan, TX, United States 
Area:
Protein chemistry, genetics
Website:
https://medicine.tamu.edu/faculty/pace.html
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85 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2014 Pace CN, Fu H, Lee Fryar K, Landua J, Trevino SR, Schell D, Thurlkill RL, Imura S, Scholtz JM, Gajiwala K, Sevcik J, Urbanikova L, Myers JK, Takano K, Hebert EJ, et al. Contribution of hydrogen bonds to protein stability. Protein Science : a Publication of the Protein Society. 23: 652-61. PMID 24591301 DOI: 10.1002/Pro.2449  0.653
2012 Kramer RM, Shende VR, Motl N, Pace CN, Scholtz JM. Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility. Biophysical Journal. 102: 1907-15. PMID 22768947 DOI: 10.1016/J.Bpj.2012.01.060  0.637
2011 Pace CN, Fu H, Fryar KL, Landua J, Trevino SR, Shirley BA, Hendricks MM, Iimura S, Gajiwala K, Scholtz JM, Grimsley GR. Contribution of hydrophobic interactions to protein stability. Journal of Molecular Biology. 408: 514-28. PMID 21377472 DOI: 10.1016/J.Jmb.2011.02.053  0.683
2010 Fu H, Grimsley G, Scholtz JM, Pace CN. Increasing protein stability: importance of DeltaC(p) and the denatured state. Protein Science : a Publication of the Protein Society. 19: 1044-52. PMID 20340133 DOI: 10.1002/Pro.381  0.65
2010 McLean JR, McLean JA, Wu Z, Becker C, Pérez LM, Pace CN, Scholtz JM, Russell DH. Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites. The Journal of Physical Chemistry. B. 114: 809-16. PMID 20000372 DOI: 10.1021/Jp9105103  0.54
2009 Scholtz JM, Grimsley GR, Pace CN. Solvent denaturation of proteins and interpretations of the m value. Methods in Enzymology. 466: 549-65. PMID 21609876 DOI: 10.1016/S0076-6879(09)66023-7  0.662
2009 Fu H, Grimsley GR, Razvi A, Scholtz JM, Pace CN. Increasing protein stability by improving beta-turns. Proteins. 77: 491-8. PMID 19626709 DOI: 10.1002/Prot.22509  0.636
2009 Grimsley GR, Scholtz JM, Pace CN. A summary of the measured pK values of the ionizable groups in folded proteins. Protein Science : a Publication of the Protein Society. 18: 247-51. PMID 19177368 DOI: 10.1002/Pro.19  0.602
2009 Pace CN, Grimsley GR, Scholtz JM. Protein ionizable groups: pK values and their contribution to protein stability and solubility. The Journal of Biological Chemistry. 284: 13285-9. PMID 19164280 DOI: 10.1074/Jbc.R800080200  0.658
2009 Shaw KL, Scholtz JM, Pace CN, Grimsley GR. Determining the conformational stability of a protein using urea denaturation curves. Methods in Molecular Biology (Clifton, N.J.). 490: 41-55. PMID 19157078 DOI: 10.1007/978-1-59745-367-7_2  0.667
2008 Ilinskaya ON, Koschinski A, Repp H, Mitkevich VA, Dreyer F, Scholtz JM, Pace CN, Makarov AA. RNase-induced apoptosis: fate of calcium-activated potassium channels. Biochimie. 90: 717-25. PMID 18291113 DOI: 10.1016/J.Biochi.2008.01.010  0.474
2008 Trevino SR, Scholtz JM, Pace CN. Measuring and increasing protein solubility. Journal of Pharmaceutical Sciences. 97: 4155-66. PMID 18240286 DOI: 10.1002/Jps.21327  0.648
2008 Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD, Pace CN. Peptide sequence and conformation strongly influence tryptophan fluorescence. Biophysical Journal. 94: 2280-7. PMID 18065477 DOI: 10.1529/Biophysj.107.116921  0.554
2008 Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD, Pace CN. Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa. Biophysical Journal. 94: 2288-96. PMID 18065473 DOI: 10.1529/Biophysj.107.116954  0.63
2008 Pace CN, Grimsley GR, Scholtz JM. Denaturation of Proteins by Urea and Guanidine Hydrochloride Protein Folding Handbook. 1: 45-69. DOI: 10.1002/9783527619498.ch3  0.632
2007 Trevino SR, Schaefer S, Scholtz JM, Pace CN. Increasing protein conformational stability by optimizing beta-turn sequence. Journal of Molecular Biology. 373: 211-8. PMID 17765922 DOI: 10.1016/J.Jmb.2007.07.061  0.593
2007 Trevino SR, Scholtz JM, Pace CN. Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa. Journal of Molecular Biology. 366: 449-60. PMID 17174328 DOI: 10.1016/J.Jmb.2006.10.026  0.611
2006 Grimsley GR, Huyghues-Despointes BM, Pace CN, Scholtz JM. Measuring the conformational stability of a protein by NMR. Csh Protocols. 2006. PMID 22485641 DOI: 10.1101/pdb.prot4244  0.645
2006 Grimsley GR, Huyghues-Despointes BM, Pace CN, Scholtz JM. Determining a thermal unfolding curve. Csh Protocols. 2006. PMID 22485640 DOI: 10.1101/Pdb.Prot4243  0.518
2006 Grimsley GR, Huyghues-Despointes BM, Pace CN, Scholtz JM. Determining a urea or guanidinium chloride unfolding curve. Csh Protocols. 2006. PMID 22485639 DOI: 10.1101/Pdb.Prot4242  0.554
2006 Grimsley GR, Huyghues-Despointes BM, Pace CN, Scholtz JM. Preparation of urea and guanidinium chloride stock solutions for measuring denaturant-induced unfolding curves. Csh Protocols. 2006. PMID 22485638 DOI: 10.1101/Pdb.Prot4241  0.531
2006 Thurlkill RL, Grimsley GR, Scholtz JM, Pace CN. Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins. Journal of Molecular Biology. 362: 594-604. PMID 16934292 DOI: 10.1016/J.Jmb.2006.07.056  0.624
2006 Thurlkill RL, Grimsley GR, Scholtz JM, Pace CN. pK values of the ionizable groups of proteins. Protein Science : a Publication of the Protein Society. 15: 1214-8. PMID 16597822 DOI: 10.1110/Ps.051840806  0.597
2006 Schell D, Tsai J, Scholtz JM, Pace CN. Hydrogen bonding increases packing density in the protein interior. Proteins. 63: 278-82. PMID 16353166 DOI: 10.1002/Prot.20826  0.62
2005 Thurlkill RL, Cross DA, Scholtz JM, Pace CN. pKa of fentanyl varies with temperature: implications for acid-base management during extremes of body temperature. Journal of Cardiothoracic and Vascular Anesthesia. 19: 759-62. PMID 16326301 DOI: 10.1053/J.Jvca.2004.11.039  0.484
2005 Trevino SR, Gokulan K, Newsom S, Thurlkill RL, Shaw KL, Mitkevich VA, Makarov AA, Sacchettini JC, Scholtz JM, Pace CN. Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. Journal of Molecular Biology. 354: 967-78. PMID 16288913 DOI: 10.1016/J.Jmb.2005.09.091  0.634
2005 Trefethen JM, Pace CN, Scholtz JM, Brems DN. Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa. Protein Science : a Publication of the Protein Society. 14: 1934-8. PMID 15937282 DOI: 10.1110/Ps.051401905  0.609
2005 Laurents DV, Scholtz JM, Rico M, Pace CN, Bruix M. Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange. Biochemistry. 44: 7644-55. PMID 15909979 DOI: 10.1021/Bi050142B  0.651
2004 Grimsley GR, Pace CN. Spectrophotometric determination of protein concentration. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 3.1. PMID 18429266 DOI: 10.1002/0471140864.ps0301s33  0.306
2004 Alston RW, Urbanikova L, Sevcik J, Lasagna M, Reinhart GD, Scholtz JM, Pace CN. Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa. Biophysical Journal. 87: 4036-47. PMID 15377518 DOI: 10.1529/Biophysj.104.050377  0.608
2004 Pace CN, Treviño S, Prabhakaran E, Scholtz JM. Protein structure, stability and solubility in water and other solvents. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 359: 1225-34; discussion . PMID 15306378 DOI: 10.1098/Rstb.2004.1500  0.75
2003 Takano K, Scholtz JM, Sacchettini JC, Pace CN. The contribution of polar group burial to protein stability is strongly context-dependent. The Journal of Biological Chemistry. 278: 31790-5. PMID 12799387 DOI: 10.1074/Jbc.M304177200  0.64
2003 Huyghues-Despointes BM, Thurlkill RL, Daily MD, Schell D, Briggs JM, Antosiewicz JM, Pace CN, Scholtz JM. pK values of histidine residues in ribonuclease Sa: effect of salt and net charge. Journal of Molecular Biology. 325: 1093-105. PMID 12527310 DOI: 10.1016/S0022-2836(02)01274-3  0.624
2003 Laurents DV, Huyghues-Despointes BM, Bruix M, Thurlkill RL, Schell D, Newsom S, Grimsley GR, Shaw KL, Treviño S, Rico M, Briggs JM, Antosiewicz JM, Scholtz JM, Pace CN. Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2). Journal of Molecular Biology. 325: 1077-92. PMID 12527309 DOI: 10.1016/S0022-2836(02)01273-1  0.592
2002 Pace CN, Huyghues-Despointes BM, Briggs JM, Grimsley GR, Scholtz JM. Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1. Biophysical Chemistry. 101: 211-9. PMID 12488002 DOI: 10.1016/S0301-4622(02)00192-8  0.583
2001 Pace CN, Horn G, Hebert EJ, Bechert J, Shaw K, Urbanikova L, Scholtz JM, Sevcik J. Tyrosine hydrogen bonds make a large contribution to protein stability. Journal of Molecular Biology. 312: 393-404. PMID 11554795 DOI: 10.1006/jmbi.2001.4956  0.655
2001 Huyghues-Despointes BM, Pace CN, Englander SW, Scholtz JM. Measuring the conformational stability of a protein by hydrogen exchange. Methods in Molecular Biology (Clifton, N.J.). 168: 69-92. PMID 11357629 DOI: 10.1385/1-59259-193-0:069  0.66
2001 Pace CN. Polar group burial contributes more to protein stability than nonpolar group burial. Biochemistry. 40: 310-3. PMID 11148023 DOI: 10.1021/bi001574j  0.382
2000 Pace CN, Alston RW, Shaw KL. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability Protein Science. 9: 1395-1398. PMID 10933506 DOI: 10.1110/Ps.9.7.1395  0.323
1999 Huyghues-Despointes BM, Langhorst U, Steyaert J, Pace CN, Scholtz JM. Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix. Biochemistry. 38: 16481-90. PMID 10600109 DOI: 10.1021/bi9919450  0.635
1999 Giletto A, Pace CN. Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. Biochemistry. 38: 13379-84. PMID 10529213 DOI: 10.1021/bi991422s  0.351
1999 Giletto A, Pace CN. Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. Biochemistry. 38: 13379-84. PMID 10529213 DOI: 10.1021/bi991422s  0.351
1999 Huyghues-Despointes BM, Scholtz JM, Pace CN. Protein conformational stabilities can be determined from hydrogen exchange rates. Nature Structural Biology. 6: 910-2. PMID 10504722 DOI: 10.1038/13273  0.616
1999 Grimsley GR, Shaw KL, Fee LR, Alston RW, Huyghues-Despointes BM, Thurlkill RL, Scholtz JM, Pace CN. Increasing protein stability by altering long-range coulombic interactions. Protein Science : a Publication of the Protein Society. 8: 1843-9. PMID 10493585 DOI: 10.1110/Ps.8.9.1843  0.666
1999 Krishnan P, Hocking AM, Scholtz JM, Pace CN, Holik KK, McQuillan DJ. Distinct secondary structures of the leucine-rich repeat proteoglycans decorin and biglycan. Glycosylation-dependent conformational stability. The Journal of Biological Chemistry. 274: 10945-50. PMID 10196174 DOI: 10.1074/Jbc.274.16.10945  0.63
1998 Hebert EJ, Giletto A, Sevcik J, Urbanikova L, Wilson KS, Dauter Z, Pace CN. Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1. Biochemistry. 37: 16192-200. PMID 9819211 DOI: 10.1021/bi9815243  0.398
1998 Pace CN, Scholtz JM. A helix propensity scale based on experimental studies of peptides and proteins. Biophysical Journal. 75: 422-7. PMID 9649402 DOI: 10.1016/S0006-3495(98)77529-0  0.614
1998 Pace CN, Hebert EJ, Shaw KL, Schell D, Both V, Krajcikova D, Sevcik J, Wilson KS, Dauter Z, Hartley RW, Grimsley GR. Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3. Journal of Molecular Biology. 279: 271-86. PMID 9636716 DOI: 10.1006/Jmbi.1998.1760  0.305
1998 Myers JK, Pace CN, Scholtz JM. Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1. Protein Science : a Publication of the Protein Society. 7: 383-8. PMID 9521115 DOI: 10.1002/pro.5560070219  0.586
1997 Grimsley JK, Scholtz JM, Pace CN, Wild JR. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry. 36: 14366-74. PMID 9398154 DOI: 10.1021/bi971596e  0.639
1997 Myers JK, Pace CN, Scholtz JM. Helix propensities are identical in proteins and peptides. Biochemistry. 36: 10923-9. PMID 9283083 DOI: 10.1021/bi9707180  0.611
1997 Myers JK, Pace CN, Scholtz JM. A direct comparison of helix propensity in proteins and peptides. Proceedings of the National Academy of Sciences of the United States of America. 94: 2833-7. PMID 9096306 DOI: 10.1073/Pnas.94.7.2833  0.648
1996 Myers JK, Smith JS, Pace CN, Scholtz JM. The alpha-helix of ribonuclease T1 as an independent stability unit: direct comparison of peptide and protein stability. Journal of Molecular Biology. 263: 390-5. PMID 8918595 DOI: 10.1006/Jmbi.1996.0583  0.665
1996 Myers JK, Pace CN. Hydrogen bonding stabilizes globular proteins. Biophysical Journal. 71: 2033-9. PMID 8889177 DOI: 10.1016/S0006-3495(96)79401-8  0.327
1996 Pace CN, Shirley BA, McNutt M, Gajiwala K. Forces contributing to the conformational stability of proteins. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 75-83. PMID 8566551 DOI: 10.1096/fasebj.10.1.8566551  0.402
1996 Pace CN, Shirley BA, McNutt M, Gajiwala K. Forces contributing to the conformational stability of proteins. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 75-83. PMID 8566551 DOI: 10.1096/fasebj.10.1.8566551  0.402
1995 Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Science : a Publication of the Protein Society. 4: 2411-23. PMID 8563639 DOI: 10.1002/pro.5560041120  0.346
1995 Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Science : a Publication of the Protein Society. 4: 2411-23. PMID 8563639 DOI: 10.1002/pro.5560041120  0.346
1995 Myers JK, Pace CN, Scholtz JM. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Science : a Publication of the Protein Society. 4: 2138-48. PMID 8535251 DOI: 10.1002/pro.5560041020  0.599
1994 Yu Y, Makhatadze GI, Pace CN, Privalov PL. Energetics of ribonuclease T1 structure Biochemistry. 33: 3312-3319. PMID 8136367 DOI: 10.1021/Bi00177A023  0.327
1993 Mullins LS, Pace CN, Raushel FM. Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopy. Biochemistry. 32: 6152-6. PMID 8512924 DOI: 10.1021/bi00075a006  0.308
1992 Shirley BA, Stanssens P, Hahn U, Pace CN. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry. 31: 725-32. PMID 1731929 DOI: 10.1021/bi00118a013  0.33
1992 Pace CN. Contribution of the hydrophobic effect to globular protein stability. Journal of Molecular Biology. 226: 29-35. PMID 1619660 DOI: 10.1016/0022-2836(92)90121-y  0.362
1992 Pace CN. Contribution of the hydrophobic effect to globular protein stability. Journal of Molecular Biology. 226: 29-35. PMID 1619660 DOI: 10.1016/0022-2836(92)90121-y  0.362
1991 McNutt M, Mullins LS, Raushel FM, Pace CN. Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala. Biochemistry. 29: 7572-6. PMID 1980207 DOI: 10.1021/bi00485a005  0.369
1991 Pace CN, Heinemann U, Hahn U, Saenger W. Ribonuclease T1: Structure, Function, and Stability Angewandte Chemie. 30: 343-360. DOI: 10.1002/Anie.199103433  0.41
1990 Pace CN, Laurents DV, Thomson JA. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry. 29: 2564-72. PMID 2110472 DOI: 10.1021/bi00462a019  0.338
1990 Pace CN, Laurents DV, Thomson JA. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry. 29: 2564-72. PMID 2110472 DOI: 10.1021/bi00462a019  0.338
1990 Pace CN. Conformational stability of globular proteins. Trends in Biochemical Sciences. 15: 14-7. PMID 2107612 DOI: 10.1016/0968-0004(90)90124-t  0.403
1990 Pace CN. Conformational stability of globular proteins. Trends in Biochemical Sciences. 15: 14-7. PMID 2107612 DOI: 10.1016/0968-0004(90)90124-t  0.403
1990 Pace CN. Measuring and increasing protein stability. Trends in Biotechnology. 8: 93-8. PMID 1367432 DOI: 10.1016/0167-7799(90)90146-o  0.351
1990 Pace CN. Measuring and increasing protein stability. Trends in Biotechnology. 8: 93-8. PMID 1367432 DOI: 10.1016/0167-7799(90)90146-o  0.351
1989 Thomson JA, Shirley BA, Grimsley GR, Pace CN. Conformational stability and mechanism of folding of ribonuclease T1. The Journal of Biological Chemistry. 264: 11614-20. PMID 2745409  0.306
1989 Thomson JA, Shirley BA, Grimsley GR, Pace CN. Conformational stability and mechanism of folding of ribonuclease T1. The Journal of Biological Chemistry. 264: 11614-20. PMID 2745409  0.306
1988 Pace CN, Grimsley GR, Thomson JA, Barnett BJ. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. The Journal of Biological Chemistry. 263: 11820-5. PMID 2457027  0.315
1988 Pace CN, Grimsley GR, Thomson JA, Barnett BJ. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. The Journal of Biological Chemistry. 263: 11820-5. PMID 2457027  0.315
1984 Pace CN, Barrett AJ. Kinetics of tryptic hydrolysis of the arginine-valine bond in folded and unfolded ribonuclease T1 Biochemical Journal. 219: 411-417. PMID 6430267  0.37
1983 Pace CN. Protein conformations and their stability Journal of the American Oil Chemists' Society. 60: 970-975. DOI: 10.1007/BF02660210  0.4
1981 Pace CN, Fisher LM, Cupo JF. Globular protein stability: Aspects of interest in protein turnover Acta Biologica Et Medica Germanica. 40: 1385-1392. PMID 6282021  0.368
1980 Pace CN, McGrath T. Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation. The Journal of Biological Chemistry. 255: 3862-5. PMID 7372654  0.301
1980 Pace CN, McGrath T. Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation. The Journal of Biological Chemistry. 255: 3862-5. PMID 7372654  0.301
1979 Pace CN, Vanderburg KE. Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin. Biochemistry. 18: 288-92. PMID 570408 DOI: 10.1021/BI00569A008  0.4
1975 Pace CN. The stability of globular proteins. Crc Critical Reviews in Biochemistry. 3: 1-43. PMID 238787 DOI: 10.3109/10409237509102551  0.374
1971 Alexander SS, Pace CN. A comparison of the denaturation of bovine β-lactoglobulins A and B and goat β-lactoglobulin Biochemistry. 10: 2738-2743. PMID 5558696 DOI: 10.1021/bi00790a013  0.312
1968 Hammes GG, Pace CN. Ultrasonic absorption measurements in aqueous solutions of glycine, diglycine, and triglycine. The Journal of Physical Chemistry. 72: 2227-30. PMID 5650147 DOI: 10.1021/j100852a060  0.42
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