메뉴 건너뛰기




Volumn 55, Issue 3, 2004, Pages 689-704

The Determinants of Carboxyl pKa Values in Turkey Ovomucoid Third Domain

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; OVOMUCOID; SERINE PROTEINASE INHIBITOR;

EID: 2942677105     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20032     Document Type: Article
Times cited : (82)

References (90)
  • 1
    • 0036681440 scopus 로고    scopus 로고
    • Empirical relationships between protein structure and carboxyl pK(a) values in proteins
    • Forsyth WR, Antosiewiez JM, Robertson AD. Empirical relationships between protein structure and carboxyl pK(a) values in proteins. Proteins 2002;48:388-403.
    • (2002) Proteins , vol.48 , pp. 388-403
    • Forsyth, W.R.1    Antosiewiez, J.M.2    Robertson, A.D.3
  • 2
    • 0036783381 scopus 로고    scopus 로고
    • Variability in the pKa of histidine side-chains correlates with burial within proteins
    • Edgcomb SP, Murphy KP. Variability in the pKa of histidine side-chains correlates with burial within proteins. Proteins 2002; 49:1-6.
    • (2002) Proteins , vol.49 , pp. 1-6
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 3
    • 0036001159 scopus 로고    scopus 로고
    • Structural basis of perturbed p(Ka) values of catalytic groups in enzyme active sites
    • Harris TK, Turner GJ. Structural basis of perturbed p(Ka) values of catalytic groups in enzyme active sites. IUBMB Life 2002;53:85-98.
    • (2002) IUBMB Life , vol.53 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 4
    • 0034855331 scopus 로고    scopus 로고
    • The determinants of alpha-amylase pH-activity profiles
    • Nielsen JE, Borchert TV, Vriend G. The determinants of alpha-amylase pH-activity profiles. Protein Eng 2001;14:505-512.
    • (2001) Protein Eng , vol.14 , pp. 505-512
    • Nielsen, J.E.1    Borchert, T.V.2    Vriend, G.3
  • 5
    • 0023660015 scopus 로고
    • Electrostatic effects on modification of charged groups in the active-site cleft of subtilisin by protein engineering
    • Russell AJ, Thomas PG, Fersht AR. Electrostatic effects on modification of charged groups in the active-site cleft of subtilisin by protein engineering. J Mol Biol 1987;193:803-813.
    • (1987) J Mol Biol , vol.193 , pp. 803-813
    • Russell, A.J.1    Thomas, P.G.2    Fersht, A.R.3
  • 6
    • 0027257747 scopus 로고
    • Long-range surface-charge charge interactions in proteins-comparison of experimental results with calculations from a theoretical method
    • Loewenthal R, Sancho J, Reinikainen T, Fersht AR. Long-range surface-charge charge interactions in proteins-comparison of experimental results with calculations from a theoretical method. J Mol Biol 1993;232:574-583.
    • (1993) J Mol Biol , vol.232 , pp. 574-583
    • Loewenthal, R.1    Sancho, J.2    Reinikainen, T.3    Fersht, A.R.4
  • 7
    • 0034636803 scopus 로고    scopus 로고
    • Insensitivity of perturbed carboxyl pK(a) values in the ovomucoid third domain to charge replacement at a neighboring residue
    • Forsyth WR, Robertson AD. Insensitivity of perturbed carboxyl pK(a) values in the ovomucoid third domain to charge replacement at a neighboring residue. Biochemistry 2000;39:8067-8072.
    • (2000) Biochemistry , vol.39 , pp. 8067-8072
    • Forsyth, W.R.1    Robertson, A.D.2
  • 8
    • 0037129945 scopus 로고    scopus 로고
    • Electrostatic interactions in ubiquitin: Stabilization of carboxylates by lysine amino groups
    • Sundd M, Iverson N, Ibarra-Molero B, Sanchez-Ruiz JM, Robertson AD. Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. Biochemistry 2002;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
  • 9
    • 2442429974 scopus 로고    scopus 로고
    • Role of microenvironments in modulating pKa shifts in proteins
    • Mehler EL, Fuxreiter M, Garcia-Moreno B. Role of microenvironments in modulating pKa shifts in proteins. Biophys J 2002;82: 1748.
    • (2002) Biophys J , vol.82 , pp. 1748
    • Mehler, E.L.1    Fuxreiter, M.2    Garcia-Moreno, B.3
  • 10
    • 0036681396 scopus 로고    scopus 로고
    • The role of hydrophobic microenvironments in modulating pK(a) shifts in proteins
    • Mehler EL, Fuxreiter M, Simon I, Garcia-Moreno EB. The role of hydrophobic microenvironments in modulating pK(a) shifts in proteins. Proteins 2002;48:283-292.
    • (2002) Proteins , vol.48 , pp. 283-292
    • Mehler, E.L.1    Fuxreiter, M.2    Simon, I.3    Garcia-Moreno, E.B.4
  • 13
    • 0017292056 scopus 로고
    • The alpha-helix as an electric macrodipole
    • Wada A. The alpha-helix as an electric macrodipole. Adv Biophys 1976;9:1-63.
    • (1976) Adv Biophys , vol.9 , pp. 1-63
    • Wada, A.1
  • 14
    • 0021978310 scopus 로고
    • The role of the alpha-helix dipole in protein function and structure
    • Hol WGJ. The role of the alpha-helix dipole in protein function and structure. Prog Biophys Mol Biol 1985;45:149-195.
    • (1985) Prog Biophys Mol Biol , vol.45 , pp. 149-195
    • Hol, W.G.J.1
  • 15
    • 0024290472 scopus 로고
    • Amino-acid preferences for specific locations at the ends of alpha-helices
    • Richardson JS, Richardson DC. Amino-acid preferences for specific locations at the ends of alpha-helices. Science 1988;240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 16
    • 0026590664 scopus 로고
    • Histidine-residues at the N-termini and C-termini of alpha-helices-perturbed Pkas and protein stability
    • Sancho J, Serrano L, Fersht AR. Histidine-residues at the N-termini and C-termini of alpha-helices-perturbed Pkas and protein stability. Biochemistry 1992;31:2253-2258.
    • (1992) Biochemistry , vol.31 , pp. 2253-2258
    • Sancho, J.1    Serrano, L.2    Fersht, A.R.3
  • 17
    • 0028886558 scopus 로고
    • Ionization of cysteine residues at the termini of model alpha-helical peptides-relevance to unusual thiol Pk(a) values in proteins of the thioredoxin family
    • Kortemme T, Creighton TE. Ionization of cysteine residues at the termini of model alpha-helical peptides-relevance to unusual thiol Pk(a) values in proteins of the thioredoxin family. J Mol Biol 1995;253:799-812.
    • (1995) J Mol Biol , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 18
    • 0000467270 scopus 로고
    • Electrostatic basis of structure-function correlation in proteins
    • Warshel A. Electrostatic basis of structure-function correlation in proteins. Acc Chem Res 1981;14:284-290.
    • (1981) Acc Chem Res , vol.14 , pp. 284-290
    • Warshel, A.1
  • 19
    • 0025197061 scopus 로고
    • pkas of ionizable groups in proteins - Atomic detail from a continuum electrostatic model
    • Bashford D, Karplus M. pkas of Ionizable groups in proteins - atomic detail from a continuum electrostatic model. Biochemistry 1990;29:10219-10225.
    • (1990) Biochemistry , vol.29 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 21
    • 0028305457 scopus 로고
    • Prediction of Ph-dependent properties of proteins
    • Antosiewicz J, McCammon JA, Gilson MK. Prediction of Ph-dependent properties of proteins. J Mol Biol 1994;238:415-436.
    • (1994) J Mol Biol , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3
  • 23
    • 0000671518 scopus 로고    scopus 로고
    • Consistent calculations of pK(a)'s of ionizable residues in proteins: Semi-microscopic and microscopic approaches
    • Sham YY, Chu ZT, Warshel A. Consistent calculations of pK(a)'s of ionizable residues in proteins: semi-microscopic and microscopic approaches. J Phys Chem B 1997;101:4458-4472.
    • (1997) J Phys Chem B , vol.101 , pp. 4458-4472
    • Sham, Y.Y.1    Chu, Z.T.2    Warshel, A.3
  • 24
    • 0028169692 scopus 로고
    • Intrinsic pkas of ionizable residues in proteins-an explicit solvent calculation for lysozyme
    • Delbuono GS, Figueirido FE, Levy RM. Intrinsic pkas of ionizable residues in proteins-an explicit solvent calculation for lysozyme. Proteins 1994;20:85-97.
    • (1994) Proteins , vol.20 , pp. 85-97
    • Delbuono, G.S.1    Figueirido, F.E.2    Levy, R.M.3
  • 25
    • 0023060081 scopus 로고
    • Free-energy of charges in solvated proteins-microscopic calculations using a reversible charging process
    • Warshel A, Sussman F, King G. Free-energy of charges in solvated proteins-microscopic calculations using a reversible charging process. Biochemistry 1986;25:8368-8372.
    • (1986) Biochemistry , vol.25 , pp. 8368-8372
    • Warshel, A.1    Sussman, F.2    King, G.3
  • 26
    • 7044239742 scopus 로고
    • Free-energy calculations-applications to chemical and biochemical phenomena
    • Kollman P. Free-energy calculations-applications to chemical and biochemical phenomena. Chem Rev 1993;93:2395-2417.
    • (1993) Chem Rev , vol.93 , pp. 2395-2417
    • Kollman, P.1
  • 27
    • 0033012333 scopus 로고    scopus 로고
    • A self-consistent, microenvironment modulated screened Coulomb potential approximation to calculate pH-dependent electrostatic effects in proteins
    • Mehler EL, Guarnieri F. A self-consistent, microenvironment modulated screened Coulomb potential approximation to calculate pH-dependent electrostatic effects in proteins. Biophys J 1999;77:3-22.
    • (1999) Biophys J , vol.77 , pp. 3-22
    • Mehler, E.L.1    Guarnieri, F.2
  • 28
    • 0032769471 scopus 로고    scopus 로고
    • A fast and simple method to calculate protonation states in proteins
    • Sandberg L, Edholm O. A fast and simple method to calculate protonation states in proteins. Proteins 1999;36:474-483.
    • (1999) Proteins , vol.36 , pp. 474-483
    • Sandberg, L.1    Edholm, O.2
  • 29
    • 0022522422 scopus 로고
    • Calculation of electrostatic interactions in proteins
    • Matthew JB, Gurd FRN. Calculation of electrostatic interactions in proteins. Methods Enzymol 1986;130:413-436.
    • (1986) Methods Enzymol , vol.130 , pp. 413-436
    • Matthew, J.B.1    Gurd, F.R.N.2
  • 30
    • 0035370422 scopus 로고    scopus 로고
    • Optimizing the hydrogen-bond network in Poisson-Boltzmann equation-based pK(a) calculations
    • Nielsen JE, Vriend G. Optimizing the hydrogen-bond network in Poisson-Boltzmann equation-based pK(a) calculations. Proteins 2001;43:403-412.
    • (2001) Proteins , vol.43 , pp. 403-412
    • Nielsen, J.E.1    Vriend, G.2
  • 31
    • 0035451052 scopus 로고    scopus 로고
    • What are the dielectric "constants" of proteins and how to validate electrostatic models?
    • Schutz CN, Warshel A. What are the dielectric "constants" of proteins and how to validate electrostatic models? Proteins 2001; 44:400-417.
    • (2001) Proteins , vol.44 , pp. 400-417
    • Schutz, C.N.1    Warshel, A.2
  • 33
    • 0037305552 scopus 로고    scopus 로고
    • On the evaluation and optimization of protein X-ray structures for pKa calculations
    • Nielsen JE, McCammon JA. On the evaluation and optimization of protein X-ray structures for pKa calculations. Protein Sci 2003;12:313-326.
    • (2003) Protein Sci , vol.12 , pp. 313-326
    • Nielsen, J.E.1    McCammon, J.A.2
  • 34
    • 0036787760 scopus 로고    scopus 로고
    • Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins
    • Georgescu RE, Alexov EG, Gunner MR. Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins. Biophys J 2002;83:1731-1748.
    • (2002) Biophys J , vol.83 , pp. 1731-1748
    • Georgescu, R.E.1    Alexov, E.G.2    Gunner, M.R.3
  • 35
    • 0035960203 scopus 로고    scopus 로고
    • Conformational averaging in pK calculations: Improvement and limitations in prediction of ionization properties of proteins
    • Koumanov A, Karshikoff A, Friis EP, Borchert TV. Conformational averaging in pK calculations: improvement and limitations in prediction of ionization properties of proteins. J Phys Chem B 2001;105:9339-9344.
    • (2001) J Phys Chem B , vol.105 , pp. 9339-9344
    • Koumanov, A.1    Karshikoff, A.2    Friis, E.P.3    Borchert, T.V.4
  • 36
    • 0031670370 scopus 로고    scopus 로고
    • Improving the accuracy of protein pK(a) calculations: Conformational averaging versus the average structure
    • van Vlijmen HWT, Schaefer M, Karplus M. Improving the accuracy of protein pK(a) calculations: conformational averaging versus the average structure. Proteins 1998;33:145-158.
    • (1998) Proteins , vol.33 , pp. 145-158
    • Van Vlijmen, H.W.T.1    Schaefer, M.2    Karplus, M.3
  • 37
    • 0031564641 scopus 로고    scopus 로고
    • Modeling of protein conformational fluctuations in pK(a) predictions
    • Zhou HX, Vijayakumar M. Modeling of protein conformational fluctuations in pK(a) predictions. J Mol Biol 1997;267:1002-1011.
    • (1997) J Mol Biol , vol.267 , pp. 1002-1011
    • Zhou, H.X.1    Vijayakumar, M.2
  • 38
    • 0028859420 scopus 로고
    • Conformation and hydrogen ion titration of proteins: A continuum electrostatic model with conformational flexibility
    • You TJ, Bashford D. Conformation and hydrogen ion titration of proteins: a continuum electrostatic model with conformational flexibility. Biophys J 1995;69:1721-1733.
    • (1995) Biophys J , vol.69 , pp. 1721-1733
    • You, T.J.1    Bashford, D.2
  • 39
    • 0033613164 scopus 로고    scopus 로고
    • Tanford-Kirkwood electrostatics for protein modeling
    • Havranek JJ, Harbury PB. Tanford-Kirkwood electrostatics for protein modeling. Proc Natl Acad Sci USA 1999;96:11145-11150.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11145-11150
    • Havranek, J.J.1    Harbury, P.B.2
  • 40
    • 0028951968 scopus 로고
    • Ph, ionic-strength, and temperature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid 3rd domain
    • Schaller W, Robertson AD. Ph, ionic-strength, and temperature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid 3rd domain. Biochemistry 1995;34:4714-4723.
    • (1995) Biochemistry , vol.34 , pp. 4714-4723
    • Schaller, W.1    Robertson, A.D.2
  • 41
    • 0037452862 scopus 로고    scopus 로고
    • NMR determination of pK(a) values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain
    • Song JK, Laskowski M, Qasim MA, Markley JL. NMR determination of pK(a) values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain. Biochemistry 2003;42:2847-2856.
    • (2003) Biochemistry , vol.42 , pp. 2847-2856
    • Song, J.K.1    Laskowski, M.2    Qasim, M.A.3    Markley, J.L.4
  • 42
    • 0028904906 scopus 로고
    • Hydrogen-bonds and the pH-dependence of ovomucoid 3rd domain stability
    • Swintkruse L, Robertson AD. Hydrogen-bonds and the pH-dependence of ovomucoid 3rd domain stability. Biochemistry 1995;34:4724-4732.
    • (1995) Biochemistry , vol.34 , pp. 4724-4732
    • Swintkruse, L.1    Robertson, A.D.2
  • 43
    • 0032537485 scopus 로고    scopus 로고
    • Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain
    • Forsyth WR, Gilson MK, Antosiewicz J, Jaren OR, Robertson AD. Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain. Biochemistry 1998;37:8643-8652.
    • (1998) Biochemistry , vol.37 , pp. 8643-8652
    • Forsyth, W.R.1    Gilson, M.K.2    Antosiewicz, J.3    Jaren, O.R.4    Robertson, A.D.5
  • 44
    • 84961973524 scopus 로고    scopus 로고
    • The prediction of protein pK(a)'s using QM/MM: The pK(a) of lysine 55 in turkey ovomucoid third domain
    • Li H, Hains AW, Everts JE, Robertson AD, Jensen JH. The prediction of protein pK(a)'s using QM/MM: the pK(a) of lysine 55 in turkey ovomucoid third domain. J Phys Chem B 2002;106:3486-3494.
    • (2002) J Phys Chem B , vol.106 , pp. 3486-3494
    • Li, H.1    Hains, A.W.2    Everts, J.E.3    Robertson, A.D.4    Jensen, J.H.5
  • 45
    • 33751500123 scopus 로고
    • Absolute Pka calculations with continuum dielectric methods
    • Lim C, Bashford D, Karplus M. Absolute Pka calculations with continuum dielectric methods. J Phys Chem 1991;95:5610-5620.
    • (1991) J Phys Chem , vol.95 , pp. 5610-5620
    • Lim, C.1    Bashford, D.2    Karplus, M.3
  • 46
    • 33751159055 scopus 로고
    • Incorporating solvation effects into density-functional electronic-structure calculations
    • Chen JL, Noodleman L, Case DA, Bashford D. Incorporating solvation effects into density-functional electronic-structure calculations. J Phys Chem 1994;98:11059-11068.
    • (1994) J Phys Chem , vol.98 , pp. 11059-11068
    • Chen, J.L.1    Noodleman, L.2    Case, D.A.3    Bashford, D.4
  • 47
    • 84962440579 scopus 로고    scopus 로고
    • Incorporating solvation effects into density functional theory: Calculation of absolute acidities
    • Richardson WH, Peng C, Bashford D, Noodleman L, Case DA. Incorporating solvation effects into density functional theory: calculation of absolute acidities. Int J Quantum Chem 1997;61:207-217.
    • (1997) Int J Quantum Chem , vol.61 , pp. 207-217
    • Richardson, W.H.1    Peng, C.2    Bashford, D.3    Noodleman, L.4    Case, D.A.5
  • 48
    • 0001591264 scopus 로고    scopus 로고
    • Calculation of substituent effects on pK(a) values for pyrone and dihydropyrone inhibitors of HIV-1 protease
    • Topol IA, Burt SK, Rashin AA, Erickson JW. Calculation of substituent effects on pK(a) values for pyrone and dihydropyrone inhibitors of HIV-1 protease. J Phys Chem A 2000;104:866-872.
    • (2000) J Phys Chem A , vol.104 , pp. 866-872
    • Topol, I.A.1    Burt, S.K.2    Rashin, A.A.3    Erickson, J.W.4
  • 49
    • 0035892148 scopus 로고    scopus 로고
    • Interactions of azodicarbonamide (ADA) species with the model zinc finger site: Theoretical support of the zinc finger domain destruction in the HIV-1 nucleocapsid protein (NCp7) by ADA
    • Topol IA, Nemukhin AV, Dobrogorskaya YI, Burt SK. Interactions of azodicarbonamide (ADA) species with the model zinc finger site: theoretical support of the zinc finger domain destruction in the HIV-1 nucleocapsid protein (NCp7) by ADA. J Phys Chem B 2001;105:11341-11350.
    • (2001) J Phys Chem B , vol.105 , pp. 11341-11350
    • Topol, I.A.1    Nemukhin, A.V.2    Dobrogorskaya, Y.I.3    Burt, S.K.4
  • 50
    • 0031358013 scopus 로고    scopus 로고
    • Calculation of absolute and relative acidities of substituted imidazoles in aqueous solvent
    • Topol IA, Tawa GJ, Burt SK, Rashin AA. Calculation of absolute and relative acidities of substituted imidazoles in aqueous solvent. J Phys Chem A 1997;101:10075-10081.
    • (1997) J Phys Chem A , vol.101 , pp. 10075-10081
    • Topol, I.A.1    Tawa, G.J.2    Burt, S.K.3    Rashin, A.A.4
  • 52
    • 0035127984 scopus 로고    scopus 로고
    • First principles calculation of pK(a) values for 5-substituted uracils
    • Jang YH, Sowers LC, Cagin T, Goddard WA. First principles calculation of pK(a) values for 5-substituted uracils. J Phys Chem A 2001;105:274-280.
    • (2001) J Phys Chem A , vol.105 , pp. 274-280
    • Jang, Y.H.1    Sowers, L.C.2    Cagin, T.3    Goddard, W.A.4
  • 53
    • 84961981283 scopus 로고    scopus 로고
    • Prediction of the pK(a) of carboxylic acids using the ab initio continuum-solvation model PCM-UAHF
    • Schuurmann G, Cossi M, Barone V, Tomasi J. Prediction of the pK(a) of carboxylic acids using the ab initio continuum-solvation model PCM-UAHF. J Phys Chem A 1998;102:6706-6712.
    • (1998) J Phys Chem A , vol.102 , pp. 6706-6712
    • Schuurmann, G.1    Cossi, M.2    Barone, V.3    Tomasi, J.4
  • 54
    • 28944439105 scopus 로고    scopus 로고
    • Ab initio calculations of absolute pK(a) values in aqueous solution I. Carboxylic acids
    • da Silva CO, da Silva EC, Nascimento MAC. Ab initio calculations of absolute pK(a) values in aqueous solution I. Carboxylic acids. J Phys Chem A 1999;103:11194-11199.
    • (1999) J Phys Chem A , vol.103 , pp. 11194-11199
    • Da Silva, C.O.1    Da Silva, E.C.2    Nascimento, M.A.C.3
  • 55
    • 0034704774 scopus 로고    scopus 로고
    • Ab initio calculations of absolute pK(a) values in aqueous solution. II. Aliphatic alcohols, thiols, and halogenated carboxylic acids
    • Silva CO, da Silva EC, Nascimento MAC. Ab initio calculations of absolute pK(a) values in aqueous solution. II. Aliphatic alcohols, thiols, and halogenated carboxylic acids. J Phys Chem A 2000;104: 2402-2409.
    • (2000) J Phys Chem A , vol.104 , pp. 2402-2409
    • Silva, C.O.1    Da Silva, E.C.2    Nascimento, M.A.C.3
  • 57
    • 84962424896 scopus 로고    scopus 로고
    • Experimentation with different thermodynamic cycles used for pK(a) calculations on carboxylic acids using complete basis set and gaussian-n models combined with CPCM continuum solvation methods
    • Liptak MD, Shields GC. Experimentation with different thermodynamic cycles used for pK(a) calculations on carboxylic acids using complete basis set and gaussian-n models combined with CPCM continuum solvation methods. Int J Quantum Chem 2001;85:727-741.
    • (2001) Int J Quantum Chem , vol.85 , pp. 727-741
    • Liptak, M.D.1    Shields, G.C.2
  • 58
    • 84962359443 scopus 로고    scopus 로고
    • Accurate pK(a) calculations for carboxylic acids using complete basis set and gaussian-n models combined with CPCM continuum solvation methods
    • Liptak MD, Shields GC. Accurate pK(a) calculations for carboxylic acids using complete basis set and gaussian-n models combined with CPCM continuum solvation methods. J Am Chem Soc 2001;123:7314-7319.
    • (2001) J Am Chem Soc , vol.123 , pp. 7314-7319
    • Liptak, M.D.1    Shields, G.C.2
  • 59
    • 0037104738 scopus 로고    scopus 로고
    • Computation of pK(a) from dielectric continuum theory
    • Chipman DM. Computation of pK(a) from dielectric continuum theory. J Phys Chem A 2002;106:7413-7422.
    • (2002) J Phys Chem A , vol.106 , pp. 7413-7422
    • Chipman, D.M.1
  • 60
    • 0037149134 scopus 로고    scopus 로고
    • Accurate prediction of acidity constants in aqueous solution via density functional theory and self-consistent reaction field methods
    • Klicic JJ, Friesner RA, Liu SY, Guida WC. Accurate prediction of acidity constants in aqueous solution via density functional theory and self-consistent reaction field methods. J Phys Chem A 2002; 106:1327-1335.
    • (2002) J Phys Chem A , vol.106 , pp. 1327-1335
    • Klicic, J.J.1    Friesner, R.A.2    Liu, S.Y.3    Guida, W.C.4
  • 61
    • 0037165455 scopus 로고    scopus 로고
    • Theoretical determination of two structural forms of the active site in cadmium-containing phosphotriesterases
    • Zheng F, Zhan CG, Ornstein RL. Theoretical determination of two structural forms of the active site in cadmium-containing phosphotriesterases. J Phys Chem B 2002;106:717-722.
    • (2002) J Phys Chem B , vol.106 , pp. 717-722
    • Zheng, F.1    Zhan, C.G.2    Ornstein, R.L.3
  • 62
    • 2442509416 scopus 로고    scopus 로고
    • Computing macroscopic and microscopic pK(a) vaules of the Rieske iron-sulfur cluster using a combined electrostatic-density functional method
    • Ullmann GM, Noodleman L, Case DA. Computing macroscopic and microscopic pK(a) vaules of the Rieske iron-sulfur cluster using a combined electrostatic-density functional method. J Inorg Biochem 2001;86:464.
    • (2001) J Inorg Biochem , vol.86 , pp. 464
    • Ullmann, G.M.1    Noodleman, L.2    Case, D.A.3
  • 63
    • 0036933444 scopus 로고    scopus 로고
    • Density functional calculation of pK(a) values and redox potentials in the bovine Rieske iron-sulfur protein
    • Ullmann GM, Noodleman L, Case DA. Density functional calculation of pK(a) values and redox potentials in the bovine Rieske iron-sulfur protein. J Biol Inorg Chem 2002;7:632-639.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 632-639
    • Ullmann, G.M.1    Noodleman, L.2    Case, D.A.3
  • 66
    • 2442595497 scopus 로고    scopus 로고
    • Fayetteville, AR; sales@pqs-chem.com. z.pqs-chem.com; sales@pqs-chem.com
    • PQS version 2.4 PQS, Fayetteville, AR, http://www.pqs-chem.com; sales@pqs-chem.com. z.pqs-chem.com; sales@pqs-chem.com.
    • PQS Version 2.4 PQS
  • 67
    • 0031209054 scopus 로고    scopus 로고
    • A new integral equation formalism for the polarizable continuum model: Theoretical background and applications to isotropic and anisotropic dielectrics
    • Cances E, Mennucci B, Tomasi J. A new integral equation formalism for the polarizable continuum model: theoretical background and applications to isotropic and anisotropic dielectrics. J Chem Phys 1997;107:3032-3041.
    • (1997) J Chem Phys , vol.107 , pp. 3032-3041
    • Cances, E.1    Mennucci, B.2    Tomasi, J.3
  • 68
    • 0022801412 scopus 로고
    • X-ray crystal-structure of the complex of human-leukocyte elastase (Pmn Elastase) and the 3rd domain of the turkey ovomucoid inhibitor
    • Bode W, Wei AZ, Huber R, Meyer E, Travis J, Neumann S. X-ray crystal-structure of the complex of human-leukocyte elastase (Pmn Elastase) and the 3rd domain of the turkey ovomucoid inhibitor. EMBO J 1986;5:2453-2458.
    • (1986) EMBO J , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 69
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • Hooft RWW, Sander C, Vriend G. Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins 1996;26:363-376.
    • (1996) Proteins , vol.26 , pp. 363-376
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 70
    • 84962450193 scopus 로고    scopus 로고
    • http://www.cmbi.kun.nl/gv/servers/WIWWWI/.
  • 72
    • 0001461682 scopus 로고
    • Examination of titration behavior
    • Nozaki Y, Tanford C. Examination of titration behavior. Methods Enzymol 1967;11:715-734.
    • (1967) Methods Enzymol , vol.11 , pp. 715-734
    • Nozaki, Y.1    Tanford, C.2
  • 73
    • 0034091669 scopus 로고    scopus 로고
    • Backbone dipoles generate positive potentials in all proteins: Origins and implications of the effect
    • Gunner MR, Saleh MA, Cross E, ud-Doula A, Wise M. Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect. Biophys J 2000;78:1126-1144.
    • (2000) Biophys J , vol.78 , pp. 1126-1144
    • Gunner, M.R.1    Saleh, M.A.2    Cross, E.3    Ud-Doula, A.4    Wise, M.5
  • 75
    • 0034062925 scopus 로고    scopus 로고
    • Deterministic features of side-chain main-chain hydrogen bonds in globular protein structures
    • Eswar N, Ramakrishnan C. Deterministic features of side-chain main-chain hydrogen bonds in globular protein structures. Protein Eng 2000;13:227-238.
    • (2000) Protein Eng , vol.13 , pp. 227-238
    • Eswar, N.1    Ramakrishnan, C.2
  • 76
    • 0035964164 scopus 로고    scopus 로고
    • Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase
    • Joshi MD, Sidhu G, Nielsen JE, Brayer GD, Withers SG, McIntosh LP. Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase. Biochemistry 2001;40:10115-10139.
    • (2001) Biochemistry , vol.40 , pp. 10115-10139
    • Joshi, M.D.1    Sidhu, G.2    Nielsen, J.E.3    Brayer, G.D.4    Withers, S.G.5    McIntosh, L.P.6
  • 77
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase
    • Wang PF, McLeish MJ, Kneen MM, Lee G, Kenyon GL. An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry 2001;40:11698-11705.
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 78
    • 0030612614 scopus 로고    scopus 로고
    • Use of H-1 NMR spectroscopy and computer simulations to analyze histidine pK(a) changes in a protein tyrosine phosphatase: Experimental and theoretical determination of electrostatic properties in a small protein
    • Tishmack PA, Bashford D, Harms E, VanEtten RL. Use of H-1 NMR spectroscopy and computer simulations to analyze histidine pK(a) changes in a protein tyrosine phosphatase: experimental and theoretical determination of electrostatic properties in a small protein. Biochemistry 1997;36:11984-11994.
    • (1997) Biochemistry , vol.36 , pp. 11984-11994
    • Tishmack, P.A.1    Bashford, D.2    Harms, E.3    VanEtten, R.L.4
  • 79
    • 0036228118 scopus 로고    scopus 로고
    • Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein
    • Lee KK, Fitch CA, Garcia-Moreno B. Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein. Protein Sci 2002;11:1004-1016.
    • (2002) Protein Sci , vol.11 , pp. 1004-1016
    • Lee, K.K.1    Fitch, C.A.2    Garcia-Moreno, B.3
  • 81
    • 0032535188 scopus 로고    scopus 로고
    • Coulombic effects of remote subsites on the active site of ribonuclease A
    • Fisher BM, Schultz LW, Raines RT. Coulombic effects of remote subsites on the active site of ribonuclease A. Biochemistry 1998;37: 17386-17401.
    • (1998) Biochemistry , vol.37 , pp. 17386-17401
    • Fisher, B.M.1    Schultz, L.W.2    Raines, R.T.3
  • 82
    • 0037379163 scopus 로고    scopus 로고
    • Anion binding to a protein-protein complex lacks dependence on net charge
    • Waldron TT, Modestou MA, Murphy KP. Anion binding to a protein-protein complex lacks dependence on net charge. Protein Sci 2003;12:871-874.
    • (2003) Protein Sci , vol.12 , pp. 871-874
    • Waldron, T.T.1    Modestou, M.A.2    Murphy, K.P.3
  • 83
    • 0036890275 scopus 로고    scopus 로고
    • Consistent treatment of inter- and intramolecular polarization in molecular mechanics calculations
    • Ren PY, Ponder JW. Consistent treatment of inter- and intramolecular polarization in molecular mechanics calculations. J Comput Chem 2002;23:1497-1506.
    • (2002) J Comput Chem , vol.23 , pp. 1497-1506
    • Ren, P.Y.1    Ponder, J.W.2
  • 84
  • 86
    • 84961981991 scopus 로고    scopus 로고
    • A new definition of cavities for the computation of solvation free energies by the polarizable continuum model
    • Barone V, Cossi M, Tomasi J. A new definition of cavities for the computation of solvation free energies by the polarizable continuum model. J Chem Phys 1997;107:3210-3221.
    • (1997) J Chem Phys , vol.107 , pp. 3210-3221
    • Barone, V.1    Cossi, M.2    Tomasi, J.3
  • 87
    • 84946893847 scopus 로고
    • Electrostatic interaction of a solute with a continuum - A direct utilization of ab initio molecular potentials for the prevision of solvent effects
    • Miertus S, Scrocco E, Tomasi J. Electrostatic interaction of a solute with a continuum - a direct utilization of ab initio molecular potentials for the prevision of solvent effects. Chem Phys 1981;55:117-129.
    • (1981) Chem Phys , vol.55 , pp. 117-129
    • Miertus, S.1    Scrocco, E.2    Tomasi, J.3
  • 88
    • 33747754400 scopus 로고
    • A scaled particle theory of aqueous and nonaqueous solutions
    • Pierotti RA. A scaled particle theory of aqueous and nonaqueous solutions. Chem Rev 1979;76:717-726.
    • (1979) Chem Rev , vol.76 , pp. 717-726
    • Pierotti, R.A.1
  • 89
    • 84986533294 scopus 로고
    • Dispersion and repulsion contributions to the solvation energy-refinements to a simple computational model in the continuum approximation
    • Floris FM, Tomasi J, Ahuir JLP. Dispersion and repulsion contributions to the solvation energy-refinements to a simple computational model in the continuum approximation. J Comput Chem 1991;12:784-791.
    • (1991) J Comput Chem , vol.12 , pp. 784-791
    • Floris, F.M.1    Tomasi, J.2    Ahuir, J.L.P.3
  • 90
    • 84962440509 scopus 로고    scopus 로고
    • Reaction field effects on nitrogen shielding
    • Zhan CG, Chipman DM. Reaction field effects on nitrogen shielding. J Chem Phys 1999;110:1611-1622.
    • (1999) J Chem Phys , vol.110 , pp. 1611-1622
    • Zhan, C.G.1    Chipman, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.