| Year |
Citation |
Score |
| 2023 |
Thurlkill RL, Trevino SR, Scholtz JM, Grimsley GR. Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves. Current Protocols. 3: e723. PMID 36952496 DOI: 10.1002/cpz1.723 |
0.377 |
|
| 2014 |
Nick Pace C, Scholtz JM, Grimsley GR. Forces stabilizing proteins. Febs Letters. 588: 2177-84. PMID 24846139 DOI: 10.1016/J.Febslet.2014.05.006 |
0.526 |
|
| 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 |
0.812 |
|
| 2013 |
Grimsley GR, Trevino SR, Thurlkill RL, Scholtz JM. Determining the conformational stability of a protein from urea and thermal unfolding curves. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit28.4. PMID 23377851 DOI: 10.1002/0471140864.Ps2804S71 |
0.486 |
|
| 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 |
0.771 |
|
| 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 |
0.763 |
|
| 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 |
0.736 |
|
| 2010 |
Nick Pace C, Huyghues-Despointes BM, Fu H, Takano K, Scholtz JM, Grimsley GR. Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins. Protein Science : a Publication of the Protein Society. 19: 929-43. PMID 20198681 DOI: 10.1002/Pro.370 |
0.676 |
|
| 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 |
0.56 |
|
| 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 |
0.664 |
|
| 2009 |
Cho Y, Sagle LB, Iimura S, Zhang Y, Kherb J, Chilkoti A, Scholtz JM, Cremer PS. Hydrogen bonding of beta-turn structure is stabilized in D(2)O. Journal of the American Chemical Society. 131: 15188-93. PMID 19919159 DOI: 10.1021/Ja9040785 |
0.338 |
|
| 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 |
0.729 |
|
| 2009 |
López-Alonso JP, Diez-García F, Font J, Ribó M, Vilanova M, Scholtz JM, González C, Vottariello F, Gotte G, Libonati M, Laurents DV. Carbodiimide EDC induces cross-links that stabilize RNase A C-dimer against dissociation: EDC adducts can affect protein net charge, conformation, and activity. Bioconjugate Chemistry. 20: 1459-73. PMID 19606852 DOI: 10.1021/Bc9001486 |
0.433 |
|
| 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 |
0.607 |
|
| 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 |
0.661 |
|
| 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 |
0.671 |
|
| 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 |
0.478 |
|
| 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 |
0.651 |
|
| 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 |
0.563 |
|
| 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 |
0.645 |
|
| 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 |
0.591 |
|
| 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 |
0.6 |
|
| 2007 |
Wei Y, Huyghues-Despointes BM, Tsai J, Scholtz JM. NMR study and molecular dynamics simulations of optimized beta-hairpin fragments of protein G. Proteins. 69: 285-96. PMID 17600831 DOI: 10.1002/Prot.21494 |
0.466 |
|
| 2007 |
Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, Zhu A, Scholtz JM, Makarov DE, Movileanu L. Single-molecule electrophoresis of beta-hairpin peptides by electrical recordings and Langevin dynamics simulations. The Journal of Physical Chemistry. B. 111: 3332-5. PMID 17388500 DOI: 10.1021/Jp071364H |
0.401 |
|
| 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 |
0.612 |
|
| 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 |
0.602 |
|
| 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 |
0.52 |
|
| 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 |
0.556 |
|
| 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 |
0.52 |
|
| 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 |
0.637 |
|
| 2006 |
Razvi A, Scholtz JM. Lessons in stability from thermophilic proteins. Protein Science : a Publication of the Protein Society. 15: 1569-78. PMID 16815912 DOI: 10.1110/Ps.062130306 |
0.481 |
|
| 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 |
0.593 |
|
| 2006 |
Razvi A, Scholtz JM. A thermodynamic comparison of HPr proteins from extremophilic organisms. Biochemistry. 45: 4084-92. PMID 16566582 DOI: 10.1021/Bi060038+ |
0.425 |
|
| 2006 |
Huyghues-Despointes BM, Qu X, Tsai J, Scholtz JM. Terminal ion pairs stabilize the second beta-hairpin of the B1 domain of protein G. Proteins. 63: 1005-17. PMID 16470585 DOI: 10.1002/Prot.20916 |
0.619 |
|
| 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 |
0.794 |
|
| 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 |
0.481 |
|
| 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 |
0.652 |
|
| 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 |
0.623 |
|
| 2005 |
Movileanu L, Schmittschmitt JP, Scholtz JM, Bayley H. Interactions of peptides with a protein pore. Biophysical Journal. 89: 1030-45. PMID 15923222 DOI: 10.1529/Biophysj.104.057406 |
0.774 |
|
| 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 |
0.663 |
|
| 2005 |
Sridharan S, Razvi A, Scholtz JM, Sacchettini JC. The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers. Journal of Molecular Biology. 346: 919-31. PMID 15713472 DOI: 10.1016/J.Jmb.2004.12.008 |
0.482 |
|
| 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 |
0.607 |
|
| 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 |
0.77 |
|
| 2004 |
Schmittschmitt JP, Scholtz JM. The side chain of aspartic acid 69 dictates the folding mechanism of Bacillus subtilis HPr. Biochemistry. 43: 1360-8. PMID 14756573 DOI: 10.1021/Bi0357412 |
0.787 |
|
| 2003 |
Schmittschmitt JP, Scholtz JM. The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Science : a Publication of the Protein Society. 12: 2374-8. PMID 14500896 DOI: 10.1110/Ps.03152903 |
0.777 |
|
| 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 |
0.648 |
|
| 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 |
0.804 |
|
| 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 |
0.782 |
|
| 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 |
0.591 |
|
| 2002 |
Nicholson EM, Peterson RW, Scholtz JM. A partially buried site in homologous HPr proteins is not optimized for stability. Journal of Molecular Biology. 321: 355-62. PMID 12144791 DOI: 10.1016/S0022-2836(02)00630-7 |
0.711 |
|
| 2002 |
Celinski SA, Scholtz JM. Osmolyte effects on helix formation in peptides and the stability of coiled-coils. Protein Science : a Publication of the Protein Society. 11: 2048-51. PMID 12142459 DOI: 10.1110/Ps.0211702 |
0.464 |
|
| 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 |
0.63 |
|
| 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 |
0.667 |
|
| 2001 |
Zhu H, Celinski SA, Scholtz JM, Hu JC. An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway. Protein Science : a Publication of the Protein Society. 10: 24-33. PMID 11266591 DOI: 10.1110/Ps.30901 |
0.395 |
|
| 2000 |
Zhu H, Celinski SA, Scholtz JM, Hu JC. The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil. Journal of Molecular Biology. 300: 1377-87. PMID 10903875 DOI: 10.1006/Jmbi.2000.3936 |
0.464 |
|
| 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 |
0.599 |
|
| 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 |
0.61 |
|
| 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 |
0.645 |
|
| 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 |
0.636 |
|
| 1999 |
Peterson RW, Nicholson EM, Thapar R, Klevit RE, Scholtz JM. Increased helix and protein stability through the introduction of a new tertiary hydrogen bond. Journal of Molecular Biology. 286: 1609-19. PMID 10064718 DOI: 10.1006/Jmbi.1999.2574 |
0.688 |
|
| 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 |
0.632 |
|
| 1998 |
Smith DL, Struck DK, Scholtz JM, Young R. Purification and biochemical characterization of the lambda holin. Journal of Bacteriology. 180: 2531-40. PMID 9573208 DOI: 10.1128/Jb.180.9.2531-2540.1998 |
0.374 |
|
| 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 |
0.564 |
|
| 1998 |
Smith JS, Scholtz JM. Energetics of polar side-chain interactions in helical peptides: salt effects on ion pairs and hydrogen bonds. Biochemistry. 37: 33-40. PMID 9425023 DOI: 10.1021/bi972026h |
0.359 |
|
| 1998 |
Lim D, Moye-Sherman D, Ham I, Jin S, Burgess K, Scholtz JM. 2,3-Methanoamino acid analogs of Arg stabilize secondary structures of a 13 amino acid peptide in aqueous solution Chemical Communications. 2375-2376. DOI: 10.1039/A805367G |
0.365 |
|
| 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 |
0.606 |
|
| 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 |
0.593 |
|
| 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 |
0.667 |
|
| 1997 |
Nicholson EM, Scholtz JM. Interactions at helix termini and the contributions to protein stability in the escherichia coli HPr protein Protein Engineering. 10: 30. |
0.373 |
|
| 1997 |
Huffine ME, Scholtz JM. The folding kinetics of the Eschcrichia coli form of hïstidine- contaïning phosphocarrier protein (ecHPr) Faseb Journal. 11. |
0.385 |
|
| 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 |
0.686 |
|
| 1996 |
Huffine ME, Scholtz JM. Energetic implications for protein phosphorylation. Conformational stability of HPr variants that mimic phosphorylated forms. The Journal of Biological Chemistry. 271: 28898-902. PMID 8910537 DOI: 10.1074/Jbc.271.46.28898 |
0.415 |
|
| 1996 |
Nicholson EM, Scholtz JM. Conformational stability of the Escherichia coli HPr protein: test of the linear extrapolation method and a thermodynamic characterization of cold denaturation. Biochemistry. 35: 11369-78. PMID 8784192 DOI: 10.1021/bi960863y |
0.362 |
|
| 1996 |
Thapar R, Nicholson EM, Rajagopal P, Waygood EB, Scholtz JM, Klevit RE. Influence of N-cap mutations on the structure and stability of Escherichia coli HPr. Biochemistry. 35: 11268-77. PMID 8784180 DOI: 10.1021/Bi960349S |
0.41 |
|
| 1996 |
Smith JS, Scholtz JM. Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects. Biochemistry. 35: 7292-7. PMID 8679559 DOI: 10.1021/bi960341i |
0.354 |
|
| 1995 |
Pullen K, Rajagopal P, Branchini BR, Huffine ME, Reizer J, Saier MH, Scholtz JM, Klevit RE. Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure Protein Science. 4: 2478-2486. PMID 8580838 DOI: 10.1002/Pro.5560041204 |
0.486 |
|
| 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 |
0.558 |
|
| 1995 |
Scholtz JM, Barrick D, York EJ, Stewart JM, Baldwin RL. Urea unfolding of peptide helices as a model for interpreting protein unfolding. Proceedings of the National Academy of Sciences of the United States of America. 92: 185-9. PMID 7816813 DOI: 10.1073/Pnas.92.1.185 |
0.718 |
|
| 1995 |
Scholtz JM. Conformational stability of HPr: the histidine-containing phosphocarrier protein from Bacillus subtilis. Protein Science : a Publication of the Protein Society. 4: 35-43. PMID 7773175 DOI: 10.1002/pro.5560040106 |
0.376 |
|
| 1995 |
Hammen PK, Scholtz JM, Anderson JW, Waygood EB, Klevit RE. Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy Protein Science. 4: 936-944. PMID 7663349 DOI: 10.1002/Pro.5560040513 |
0.493 |
|
| 1995 |
Scholtz JM, Robertson AD. Hydrogen exchange techniques. Methods in Molecular Biology (Clifton, N.J.). 40: 291-311. PMID 7633527 DOI: 10.1385/0-89603-301-5:291 |
0.504 |
|
| 1993 |
Huyghues-Despointes BM, Scholtz JM, Baldwin RL. Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings. Protein Science : a Publication of the Protein Society. 2: 80-5. PMID 8443591 DOI: 10.1002/Pro.5560020108 |
0.551 |
|
| 1993 |
Scholtz JM, Baldwin RL. Perchlorate-induced denaturation of ribonuclease A: investigation of possible folding intermediates. Biochemistry. 32: 4604-8. PMID 8387338 |
0.482 |
|
| 1993 |
Scholtz JM, Qian H, Robbins VH, Baldwin RL. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry. 32: 9668-76. PMID 8373771 DOI: 10.1021/Bi00088A019 |
0.594 |
|
| 1993 |
Huyghues-Despointes BM, Scholtz JM, Baldwin RL. Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide. Protein Science : a Publication of the Protein Society. 2: 1604-11. PMID 8251935 DOI: 10.1002/Pro.5560021006 |
0.621 |
|
| 1992 |
Scholtz JM, Baldwin RL. The mechanism of alpha-helix formation by peptides. Annual Review of Biophysics and Biomolecular Structure. 21: 95-118. PMID 1525475 DOI: 10.1146/Annurev.Bb.21.060192.000523 |
0.58 |
|
| 1992 |
Rohl CA, Scholtz JM, York EJ, Stewart JM, Baldwin RL. Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation. Biochemistry. 31: 1263-9. PMID 1310608 DOI: 10.1021/Bi00120A001 |
0.594 |
|
| 1991 |
Scholtz JM, Marqusee S, Baldwin RL, York EJ, Stewart JM, Santoro M, Bolen DW. Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. Proceedings of the National Academy of Sciences of the United States of America. 88: 2854-8. PMID 2011594 DOI: 10.1073/Pnas.88.7.2854 |
0.695 |
|
| 1991 |
Scholtz JM, Qian H, York EJ, Stewart JM, Baldwin RL. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers. 31: 1463-70. PMID 1814498 DOI: 10.1002/Bip.360311304 |
0.567 |
|
| 1991 |
Scholtz JM, York EJ, Stewart JM, Baldwin RL. A neutral, water-soluble, .alpha.-helical peptide: the effect of ionic strength on the helix-coil equilibrium Journal of the American Chemical Society. 113: 5102-5104. DOI: 10.1021/Ja00013A079 |
0.545 |
|
| 1991 |
Morgan BP, Scholtz JM, Ballinger MD, Zipkin ID, Bartlett PA. Differential binding energy: A detailed evaluation of the influence of hydrogen-bonding and hydrophobic groups on the inhibition of thermolysin by phosphorus-containing inhibitors Journal of the American Chemical Society. 113: 297-307. DOI: 10.1021/Ja00001A043 |
0.463 |
|
| 1989 |
Scholtz JM, Bartlett PA. Synthesis and evaluation of inhibitors for Escherichia coli carbamyl phosphate synthetase Bioorganic Chemistry. 17: 422-433. DOI: 10.1016/0045-2068(89)90043-6 |
0.419 |
|
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