-
1
-
-
0036629213
-
pH corrections in chemical denaturant solutions
-
Acevedo, O., M. Guzman-Casado, M. M. Garcia-Mira, B. Ibarra-Molero, and J. M. Sanchez-Ruiz. 2002. pH corrections in chemical denaturant solutions. Anal. Biochem. 306:158-161.
-
(2002)
Anal. Biochem.
, vol.306
, pp. 158-161
-
-
Acevedo, O.1
Guzman-Casado, M.2
Garcia-Mira, M.M.3
Ibarra-Molero, B.4
Sanchez-Ruiz, J.M.5
-
2
-
-
0026764471
-
Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures
-
Alexander, P., S. Fahnestock, T. Lee, J. Orban, and P. Bryan. 1992. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures. Biochemistry. 31:3597-3603.
-
(1992)
Biochemistry
, vol.31
, pp. 3597-3603
-
-
Alexander, P.1
Fahnestock, S.2
Lee, T.3
Orban, J.4
Bryan, P.5
-
3
-
-
0021755210
-
Protein stabilization and destabilization by guanidinium salts
-
Arakawa, T., and S. N. Timasheff. 1984. Protein stabilization and destabilization by guanidinium salts. Biochemistry. 23:5924-5929.
-
(1984)
Biochemistry
, vol.23
, pp. 5924-5929
-
-
Arakawa, T.1
Timasheff, S.N.2
-
4
-
-
0022032982
-
The stabilization of proteins by osmolytes
-
Arakawa, T., and S. N. Timasheff. 1985. The stabilization of proteins by osmolytes. Biophys. J. 47:411-414.
-
(1985)
Biophys. J.
, vol.47
, pp. 411-414
-
-
Arakawa, T.1
Timasheff, S.N.2
-
5
-
-
0029792830
-
How Hofmeister ions affect protein stability
-
Baldwin, R. L. 1996. How Hofmeister ions affect protein stability. Biophys. J. 71:2056-2063.
-
(1996)
Biophys. J.
, vol.71
, pp. 2056-2063
-
-
Baldwin, R.L.1
-
6
-
-
1942516205
-
Mathematical methods in elementary thermodynamics
-
Blinder, S. M. 1966. Mathematical methods in elementary thermodynamics. J. Chem. Ed. 43:85-92.
-
(1966)
J. Chem. Ed.
, vol.43
, pp. 85-92
-
-
Blinder, S.M.1
-
7
-
-
0035958656
-
The osmophobic effect: Natural selection of a thermodynamic force in protein folding
-
Bolen, D. W., and I. V. Baskarov. 2001. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310:955-963.
-
(2001)
J. Mol. Biol.
, vol.310
, pp. 955-963
-
-
Bolen, D.W.1
Baskarov, I.V.2
-
8
-
-
0034642225
-
Effects of guanidine hydrochloride on the proton inventory of proteins: Implications for the interpretations of protein stability
-
Bolen, D. W., and M. Yang. 2000. Effects of guanidine hydrochloride on the proton inventory of proteins: implications for the interpretations of protein stability. Biochemistry. 39:15208-15216.
-
(2000)
Biochemistry
, vol.39
, pp. 15208-15216
-
-
Bolen, D.W.1
Yang, M.2
-
9
-
-
0017187836
-
The nature of the accessible and buried surfaces in proteins
-
Chothia, C. 1976. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105:1-12.
-
(1976)
J. Mol. Biol.
, vol.105
, pp. 1-12
-
-
Chothia, C.1
-
10
-
-
0035176391
-
Thermodynamics of interactions of urea and guanidinium salts with protein surface: Relationship between solute effects on protein stability and changes in water-accessible surface area
-
Courtenay, E. S., M. W. Capp, and M. T. Record Jr. 2001. Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein stability and changes in water-accessible surface area. Protein Sci. 10:2484-2497.
-
(2001)
Protein Sci.
, vol.10
, pp. 2484-2497
-
-
Courtenay, E.S.1
Capp, M.W.2
Record Jr., M.T.3
-
11
-
-
0036303785
-
The effects of ionic strength on protein stability: The cold-shock protein family
-
Dominy, B. N., D. Perl, F. X. Schmid, and C. L. Brooks 3rd. 2002. The effects of ionic strength on protein stability: the cold-shock protein family. J. Mol. Biol. 319:541-554.
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 541-554
-
-
Dominy, B.N.1
Perl, D.2
Schmid, F.X.3
Brooks III, C.L.4
-
12
-
-
0035193201
-
pH corrections and protein ionization in water/guanidinium chloride
-
Garcia-Mira, M. M., and J. M. Sanchez-Ruiz. 2001. pH corrections and protein ionization in water/guanidinium chloride. Biophys. J. 81:3489-3502.
-
(2001)
Biophys. J.
, vol.81
, pp. 3489-3502
-
-
Garcia-Mira, M.M.1
Sanchez-Ruiz, J.M.2
-
13
-
-
0035079285
-
Heat capacity of oxidized Escherichia coli thioredoxin fragments (1-73, 74-108) and their noncovalent complex. Evidence for burial of apolar surface in protein unfolded states
-
Georgescu, R. E., M. M. Garcia-Mira, M. L. Tasayco, and J. M. Sanchez-Ruiz. 2001. Heat capacity of oxidized Escherichia coli thioredoxin fragments (1-73, 74-108) and their noncovalent complex. Evidence for burial of apolar surface in protein unfolded states. Eur. J. Biochem. 268:1477-1485.
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 1477-1485
-
-
Georgescu, R.E.1
Garcia-Mira, M.M.2
Tasayco, M.L.3
Sanchez-Ruiz, J.M.4
-
14
-
-
0016292941
-
Urea and guanidinium chloride denaturation of ribonuclease, α-chymotrypsin, and β-lactoglobulin
-
Greene, R. F., and C. N. Pace. 1974. Urea and guanidinium chloride denaturation of ribonuclease, α-chymotrypsin, and β-lactoglobulin. J. Biol. Chem. 249:5388-5393.
-
(1974)
J. Biol. Chem.
, vol.249
, pp. 5388-5393
-
-
Greene, R.F.1
Pace, C.N.2
-
15
-
-
0032872888
-
Increasing protein stability by altering long-range coulombic interactions
-
Grimsley, G. R., K. L. Shaw, L. R. Fee, R. W. Alston, B. M. Huyghues-Despointes, R. L. Thurlkill, J. M. Scholtz, and C. N. Pace. 1999. Increasing protein stability by altering long-range coulombic interactions. Protein Sci. 8:1843-1849.
-
(1999)
Protein Sci.
, vol.8
, pp. 1843-1849
-
-
Grimsley, G.R.1
Shaw, K.L.2
Fee, L.R.3
Alston, R.W.4
Huyghues-Despointes, B.M.5
Thurlkill, R.L.6
Scholtz, J.M.7
Pace, C.N.8
-
16
-
-
0038392707
-
Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of thermus thermophilus ribonuclease H
-
Guzman-Casado, M., A. Parody-Morreale, S. Robric, S. Marqusee, and J. M. Sanchez-Ruiz. 2003. Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of thermus thermophilus ribonuclease H. J. Mol. Biol. 329:731-743.
-
(2003)
J. Mol. Biol.
, vol.329
, pp. 731-743
-
-
Guzman-Casado, M.1
Parody-Morreale, A.2
Robric, S.3
Marqusee, S.4
Sanchez-Ruiz, J.M.5
-
17
-
-
0027323022
-
Guanidine hydrochloride-induced folding of proteins
-
Hagihara, Y., S. Aimoto, A. L. Fink, and Y. Goto. 1993. Guanidine hydrochloride-induced folding of proteins. J. Mol. Biol. 231:180-184.
-
(1993)
J. Mol. Biol.
, vol.231
, pp. 180-184
-
-
Hagihara, Y.1
Aimoto, S.2
Fink, A.L.3
Goto, Y.4
-
18
-
-
0014132523
-
Thioredoxin 2: Cleavage with cyanogen bromide
-
Holmgren, A., and P. Reichard. 1967. Thioredoxin 2: cleavage with cyanogen bromide. Eur. J. Biochem. 2:187-196.
-
(1967)
Eur. J. Biochem.
, vol.2
, pp. 187-196
-
-
Holmgren, A.1
Reichard, P.2
-
19
-
-
0033594989
-
Thermal versus guanidine-induced unfolding of ubiquitin. Analysis in terms of the contributions from charge-charge interactions to protein stability
-
Ibarra-Molero, B., V. V. Loladze, G. I. Makhatadze, and J. M. Sanchez-Ruiz. 1999a. Thermal versus guanidine-induced unfolding of ubiquitin. Analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry. 38:8138-8149.
-
(1999)
Biochemistry
, vol.38
, pp. 8138-8149
-
-
Ibarra-Molero, B.1
Loladze, V.V.2
Makhatadze, G.I.3
Sanchez-Ruiz, J.M.4
-
21
-
-
1942451684
-
Linkage between temperature and chemical denaturant effects on protein stability: The interpretation of calorimetrically determined m values
-
M. Doyle and J. Ladbury, editors. John Wiley & Sons, New York. In press
-
Ibarra-Molero, B., R. Perez-Jimenez, R. Godoy-Ruiz, and J. M. Sanchez-Ruiz. 2004. Linkage between temperature and chemical denaturant effects on protein stability: the interpretation of calorimetrically determined m values. In Biocalorimetry II: Applications of Calorimetry in the Biological Sciences. M. Doyle and J. Ladbury, editors. John Wiley & Sons, New York. In press.
-
(2004)
Biocalorimetry II: Applications of Calorimetry in the Biological Sciences
-
-
Ibarra-Molero, B.1
Perez-Jimenez, R.2
Godoy-Ruiz, R.3
Sanchez-Ruiz, J.M.4
-
22
-
-
0034100347
-
The sarcosine effect on protein stability: A case of nonadditivity?
-
Ibarra-Molero, B., I. M. Plaza del Pino, B. Souhail, H. O. Hammou, and J. M. Sanchez-Ruiz. 2000. The sarcosine effect on protein stability: a case of nonadditivity? Protein Sci. 9:820-826.
-
(2000)
Protein Sci.
, vol.9
, pp. 820-826
-
-
Ibarra-Molero, B.1
Plaza Del Pino, I.M.2
Souhail, B.3
Hammou, H.O.4
Sanchez-Ruiz, J.M.5
-
23
-
-
0030458930
-
A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data
-
Ibarra-Molero, B., and J. M. Sanchez-Ruiz. 1996. A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data. Biochemistry. 35: 14689-14702.
-
(1996)
Biochemistry
, vol.35
, pp. 14689-14702
-
-
Ibarra-Molero, B.1
Sanchez-Ruiz, J.M.2
-
24
-
-
0030745849
-
Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme?
-
Ibarra-Molero, B., and J. M. Sanchez-Ruiz. 1997. Are there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme? Biochemistry. 36:9616-9624.
-
(1997)
Biochemistry
, vol.36
, pp. 9616-9624
-
-
Ibarra-Molero, B.1
Sanchez-Ruiz, J.M.2
-
25
-
-
0037019469
-
A genetic algorithm to design stabilizing surface charge distributions in proteins
-
Ibarra-Molero, B., and J. M. Sanchez-Ruiz. 2002. A genetic algorithm to design stabilizing surface charge distributions in proteins. J. Phys. Chem. B. 106:6609-6613.
-
(2002)
J. Phys. Chem. B
, vol.106
, pp. 6609-6613
-
-
Ibarra-Molero, B.1
Sanchez-Ruiz, J.M.2
-
26
-
-
0035793715
-
Native hydrogen bonds in a molten globule: The apoflavodoxin thermal intermediate
-
Irun, M. P., M. M. Garcia-Mira, J. M. Sanchez-Ruiz, and J. Sancho. 2001. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate. J. Mol. Biol. 306:877-888.
-
(2001)
J. Mol. Biol.
, vol.306
, pp. 877-888
-
-
Irun, M.P.1
Garcia-Mira, M.M.2
Sanchez-Ruiz, J.M.3
Sancho, J.4
-
27
-
-
0033862774
-
Salt effects on ionization equilibria of histidines in myoglobin
-
Kao, Y. H., C. A. Fitch, S. Bhattacharya, C. J. Sarkisian, J. T. Lecomte, and B. E. Garcia-Moreno. 2000. Salt effects on ionization equilibria of histidines in myoglobin. Biophys. J. 79:1637-1654.
-
(2000)
Biophys. J.
, vol.79
, pp. 1637-1654
-
-
Kao, Y.H.1
Fitch, C.A.2
Bhattacharya, S.3
Sarkisian, C.J.4
Lecomte, J.T.5
Garcia-Moreno, B.E.6
-
28
-
-
0023649567
-
Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin
-
Kelley, R. F., W. Shalongo, M. V. Jagannadham, and E. Stellwagen. 1987. Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin. Biochemistry. 26:1406-1411.
-
(1987)
Biochemistry
, vol.26
, pp. 1406-1411
-
-
Kelley, R.F.1
Shalongo, W.2
Jagannadham, M.V.3
Stellwagen, E.4
-
29
-
-
0027240609
-
Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position
-
Ladbury, J. E., R. Wynn, H. W. Hellinga, and J. M. Sturtevant. 1993. Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. Biochemistry. 32:7526-7530.
-
(1993)
Biochemistry
, vol.32
, pp. 7526-7530
-
-
Ladbury, J.E.1
Wynn, R.2
Hellinga, H.W.3
Sturtevant, J.M.4
-
30
-
-
0037474539
-
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)
-
Laurents, D. V., B. M. Huyghues-Despointes, M. Bruix, R. L. Thurlkill, D. Schell, S. Newsom, G. R. Grimsley, K. L. Shaw, S. Trevino, M. Rico, J. M. Briggs, J. M. Antosiewicz, J. M. Scholtz, and C. N. Pace. 2003. 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). J. Mol. Biol. 325:1077-1092.
-
(2003)
J. Mol. Biol.
, vol.325
, pp. 1077-1092
-
-
Laurents, D.V.1
Huyghues-Despointes, B.M.2
Bruix, M.3
Thurlkill, R.L.4
Schell, D.5
Newsom, S.6
Grimsley, G.R.7
Shaw, K.L.8
Trevino, S.9
Rico, M.10
Briggs, J.M.11
Antosiewicz, J.M.12
Scholtz, J.M.13
Pace, C.N.14
-
31
-
-
0035107570
-
Optimization of binding electrostatics: Charge complementarity in the barnase-barstar complex
-
Lee, L. P., and B. Tidor. 2001. Optimization of binding electrostatics: charge complementarity in the barnase-barstar complex. Protein Sci. 10:362-377.
-
(2001)
Protein Sci.
, vol.10
, pp. 362-377
-
-
Lee, L.P.1
Tidor, B.2
-
32
-
-
0033554840
-
Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
-
Loladze, V. V., B. Ibarra-Molero, J. M. Sanchez-Ruiz, and G. I. Makhatadze. 1999. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry. 38:16419-16423.
-
(1999)
Biochemistry
, vol.38
, pp. 16419-16423
-
-
Loladze, V.V.1
Ibarra-Molero, B.2
Sanchez-Ruiz, J.M.3
Makhatadze, G.I.4
-
33
-
-
0038131734
-
Surface salt bridges, double-mutant cycles, and protein stability: An experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein L9
-
Luisi, D. L., C. D. Snow, J. J. Lin, Z. S. Hendsch, B. Tidor, and D. P. Raleigh. 2003. Surface salt bridges, double-mutant cycles, and protein stability: an experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein L9. Biochemistry. 42:7050-7060.
-
(2003)
Biochemistry
, vol.42
, pp. 7050-7060
-
-
Luisi, D.L.1
Snow, C.D.2
Lin, J.J.3
Hendsch, Z.S.4
Tidor, B.5
Raleigh, D.P.6
-
34
-
-
0037432563
-
Contributions of surface salt bridges to protein stability: Guidelines for protein engineering
-
Makhatadze, G. I., V. V. Loladze, D. M. Ermolenko, X. Chen, and S. T. Thomas. 2003. Contributions of surface salt bridges to protein stability: guidelines for protein engineering. J. Mol. Biol. 327:1135-1148.
-
(2003)
J. Mol. Biol.
, vol.327
, pp. 1135-1148
-
-
Makhatadze, G.I.1
Loladze, V.V.2
Ermolenko, D.M.3
Chen, X.4
Thomas, S.T.5
-
35
-
-
0031936593
-
Anion binding to the ubiquitin molecule
-
Makhatadze, G. I., M. M. Lopez, J. M. Richardson 3rd, and S. T. Thomas. 1998. Anion binding to the ubiquitin molecule. Protein Sci. 7:689-697.
-
(1998)
Protein Sci.
, vol.7
, pp. 689-697
-
-
Makhatadze, G.I.1
Lopez, M.M.2
Richardson III, J.M.3
Thomas, S.T.4
-
36
-
-
0025360593
-
Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
-
Makhatadze, G. I., and P. L. Privalov. 1990. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. J. Mol. Biol. 213:375-384.
-
(1990)
J. Mol. Biol.
, vol.213
, pp. 375-384
-
-
Makhatadze, G.I.1
Privalov, P.L.2
-
37
-
-
0026729426
-
Protein interactions with urea and guanidinium chloride. A calorimetric study
-
Makhatadze, G. I., and P. L. Privalov. 1992. Protein interactions with urea and guanidinium chloride. A calorimetric study. J. Mol. Biol. 226:491-505.
-
(1992)
J. Mol. Biol.
, vol.226
, pp. 491-505
-
-
Makhatadze, G.I.1
Privalov, P.L.2
-
38
-
-
0036307678
-
Electrostatics significantly affect the stability of designed homeodomain variants
-
Marshall, S. A., C. S. Morgan, and S. L. Mayo. 2002. Electrostatics significantly affect the stability of designed homeodomain variants. J. Mol. Biol. 316:189-199.
-
(2002)
J. Mol. Biol.
, vol.316
, pp. 189-199
-
-
Marshall, S.A.1
Morgan, C.S.2
Mayo, S.L.3
-
39
-
-
0036310988
-
Origins of the high stability of an in vitro-selected cold-shock protein
-
Martin, A., I. Kather, and F. X. Schmid. 2002. Origins of the high stability of an in vitro-selected cold-shock protein. J. Mol. Biol. 318:1341-1349.
-
(2002)
J. Mol. Biol.
, vol.318
, pp. 1341-1349
-
-
Martin, A.1
Kather, I.2
Schmid, F.X.3
-
40
-
-
0027240046
-
Stabilization of a protein by guanidinium chloride
-
Mayr, L. M., and F. X. Schmid. 1993. Stabilization of a protein by guanidinium chloride. Biochemistry. 32:7994-7998.
-
(1993)
Biochemistry
, vol.32
, pp. 7994-7998
-
-
Mayr, L.M.1
Schmid, F.X.2
-
41
-
-
0028569153
-
Protein denaturation with guanidine hydrochloride or urea provides a different esimate of stability depending on the contributions of electrostatic interactions
-
Monera, O. D., C. M. Kay, and R. S. Hodges. 1994. Protein denaturation with guanidine hydrochloride or urea provides a different esimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3:1984-1991.
-
(1994)
Protein Sci.
, vol.3
, pp. 1984-1991
-
-
Monera, O.D.1
Kay, C.M.2
Hodges, R.S.3
-
42
-
-
0028820703
-
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
-
Myers, J. K., C. N. Pace, and J. M. Scholtz. 1995. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:2138-2148.
-
(1995)
Protein Sci.
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
43
-
-
0035853162
-
Altering dimerization specificity by changes in surface electrostatics
-
Nohaile, M. J., Z. S. Hendsch, B. Tidor, and R. T. Sauer. 2001. Altering dimerization specificity by changes in surface electrostatics. Proc. Natl. Acad. Sci. USA. 98:3109-3114.
-
(2001)
Proc. Natl. Acad. Sci. USA
, vol.98
, pp. 3109-3114
-
-
Nohaile, M.J.1
Hendsch, Z.S.2
Tidor, B.3
Sauer, R.T.4
-
44
-
-
0034020833
-
Single surface stabilizer
-
Pace, C. N. 2000. Single surface stabilizer. Nat. Struct. Biol. 7:345-346.
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 345-346
-
-
Pace, C.N.1
-
45
-
-
0033852796
-
Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
-
Pace, C. N., R. W. Alston, and K. L. Shaw. 2000. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci. 9:1395-1398.
-
(2000)
Protein Sci.
, vol.9
, pp. 1395-1398
-
-
Pace, C.N.1
Alston, R.W.2
Shaw, K.L.3
-
46
-
-
0037058895
-
Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in ribonuclease T1
-
Pace, C. N., B. M. Huyghues-Despointes, J. M. Briggs, G. R. Grimsley, and J. M. Scholtz. 2002. Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in ribonuclease T1. Biophys. Chem. 101-102:211-219.
-
(2002)
Biophys. Chem.
, vol.101-102
, pp. 211-219
-
-
Pace, C.N.1
Huyghues-Despointes, B.M.2
Briggs, J.M.3
Grimsley, G.R.4
Scholtz, J.M.5
-
47
-
-
0025271463
-
pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
-
Pace, C. N., D. V. Laurents, and J. A. Thomson. 1990. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry. 29:2564-2572.
-
(1990)
Biochemistry
, vol.29
, pp. 2564-2572
-
-
Pace, C.N.1
Laurents, D.V.2
Thomson, J.A.3
-
48
-
-
0002343673
-
Measuring the conformational stability of a protein
-
T. E. Creighton, editor. IRL Press at Oxford University Press, Oxford
-
Pace, C. N., B. A. Shirley, and J. A. Thomson. 1989. Measuring the conformational stability of a protein. In Protein Structure, a Practical Approach. T. E. Creighton, editor. IRL Press at Oxford University Press, Oxford. 311-330.
-
(1989)
Protein Structure, A Practical Approach
, pp. 311-330
-
-
Pace, C.N.1
Shirley, B.A.2
Thomson, J.A.3
-
49
-
-
0034100848
-
Two exposed amino acid residues confer thermostability on a cold shock protein
-
Perl, D., U. Mueller, U. Heinemann, and F. X. Schmid. 2000. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat. Struct. Biol. 7:380-383.
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 380-383
-
-
Perl, D.1
Mueller, U.2
Heinemann, U.3
Schmid, F.X.4
-
50
-
-
0035914477
-
Electrostatic stabilization of a thermophilic cold shock protein
-
Perl, D., and F. X. Schmid. 2001. Electrostatic stabilization of a thermophilic cold shock protein. J. Mol. Biol. 313:343-357.
-
(2001)
J. Mol. Biol.
, vol.313
, pp. 343-357
-
-
Perl, D.1
Schmid, F.X.2
-
51
-
-
0021892842
-
The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices
-
Perutz, M. F., A. M. Gronenborn, G. M. Clore, J. H. Fogg, and D. T. Shih. 1985. The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices. J. Mol. Biol. 183:491-498.
-
(1985)
J. Mol. Biol.
, vol.183
, pp. 491-498
-
-
Perutz, M.F.1
Gronenborn, A.M.2
Clore, G.M.3
Fogg, J.H.4
Shih, D.T.5
-
52
-
-
0029034433
-
An osmolyte effect on the heat capacity change for protein folding
-
Plaza del Pino, I. M., and J. M. Sanchez-Ruiz. 1995. An osmolyte effect on the heat capacity change for protein folding. Biochemistry. 34:8621-8630.
-
(1995)
Biochemistry
, vol.34
, pp. 8621-8630
-
-
Plaza Del Pino, I.M.1
Sanchez-Ruiz, J.M.2
-
54
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotypsin using different denaturants
-
Santoro, M. M., and D. W. Bolen. 1988. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotypsin using different denaturants. Biochemistry. 27:8063-8068.
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
55
-
-
0026754044
-
A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
-
Santoro, M. M., and D. W. Bolen. 1992. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry. 31:4901-4907.
-
(1992)
Biochemistry
, vol.31
, pp. 4901-4907
-
-
Santoro, M.M.1
Bolen, D.W.2
-
57
-
-
0015866154
-
Environment and exposure to solvent of protein atoms. Lysozyme and insulin
-
Shrake, A., and J. A. Rupley. 1973. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79:351-372.
-
(1973)
J. Mol. Biol.
, vol.79
, pp. 351-372
-
-
Shrake, A.1
Rupley, J.A.2
-
58
-
-
0034620528
-
Rational modification of protein stability by the mutation of charged surface residues
-
Spector, S., M. Wang, S. A. Carp, J. Robblee, Z. S. Hendsch, R. Fairman, B. Tidor, and D. P. Raleigh. 2000. Rational modification of protein stability by the mutation of charged surface residues. Biochemistry. 39:872-879.
-
(2000)
Biochemistry
, vol.39
, pp. 872-879
-
-
Spector, S.1
Wang, M.2
Carp, S.A.3
Robblee, J.4
Hendsch, Z.S.5
Fairman, R.6
Tidor, B.7
Raleigh, D.P.8
-
59
-
-
0037129945
-
Electrostatic interactions in ubiquitin: Stabilization of carboxylates by lysine amino groups
-
Sundd, M., N. Iverson, B. Ibarra-Molero, J. M. Sanchez-Ruiz, and A. D. Robertson. 2002. Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. Biochemistry. 41:7586-7596.
-
(2002)
Biochemistry
, vol.41
, pp. 7586-7596
-
-
Sundd, M.1
Iverson, N.2
Ibarra-Molero, B.3
Sanchez-Ruiz, J.M.4
Robertson, A.D.5
-
60
-
-
33947468892
-
Theory of protein titration curves. I. General equations for impenetrable spheres
-
Tanford, C. N., and J. G. Kirkwood. 1957. Theory of protein titration curves. I. General equations for impenetrable spheres. J. Am. Chem. Soc. 79:5333-5339.
-
(1957)
J. Am. Chem. Soc.
, vol.79
, pp. 5333-5339
-
-
Tanford, C.N.1
Kirkwood, J.G.2
-
61
-
-
0029919676
-
Ion pairs significantly stabilize coiled-coils in the absence of electrolyte
-
Yu, Y., O. D. Monera, R. S. Hodges, and P. L. Privalov. 1996. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J. Mol. Biol. 255:367-372.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 367-372
-
-
Yu, Y.1
Monera, O.D.2
Hodges, R.S.3
Privalov, P.L.4
-
62
-
-
0037380834
-
Electrostatic contributions to the stability of a thermophilic cold shock protein
-
Zhou, H. X., and F. Dong. 2003. Electrostatic contributions to the stability of a thermophilic cold shock protein. Biophys. J. 84:2216-2222.
-
(2003)
Biophys. J.
, vol.84
, pp. 2216-2222
-
-
Zhou, H.X.1
Dong, F.2
|