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Volumn 37, Issue 4, 1999, Pages 565-575

Hydrophobicity at the surface of proteins

Author keywords

Continuum electrostatics; Farnesyltransferase farnesylpyrophosphate; HoxB1 Pbx1; Hydrophobicity map; MDM2 p53; Molecular surface; P11 annexin II; Poisson equation; Solvent accessible surface; Thrombin NAPAP

Indexed keywords

ANNEXIN; FARNESYL TRANS TRANSFERASE; PARACETAMOL; PROTEIN; PROTEIN MDM2; PROTEIN P53; THROMBIN;

EID: 0032705825     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<565::AID-PROT7>3.0.CO;2-V     Document Type: Article
Times cited : (39)

References (62)
  • 1
    • 0033559918 scopus 로고    scopus 로고
    • Hydrogen bonding, Hydrophobie interactions, and failure of the rigid receptor hypothesis
    • Davis AM, Teague SJ. Hydrogen bonding, Hydrophobie interactions, and failure of the rigid receptor hypothesis. Angew Chem Int Ed 1999;38:736-749.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 736-749
    • Davis, A.M.1    Teague, S.J.2
  • 2
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J, Chothia C. The structure of protein-protein recognition sites. J Biol Chem 1990;265:16027-16030.
    • (1990) J Biol Chem , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 3
    • 0017892708 scopus 로고
    • Role of hydrophobicity in the binding of coenzymes
    • Janin J, Chothia C. Role of hydrophobicity in the binding of coenzymes. Biochemistry, 1978;17:2943-2948.
    • (1978) Biochemistry , vol.17 , pp. 2943-2948
    • Janin, J.1    Chothia, C.2
  • 4
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • Horton N, Lewis M. Calculation of the free energy of association for protein complexes. Prot Sci 1992;1:169-181.
    • (1992) Prot Sci , vol.1 , pp. 169-181
    • Horton, N.1    Lewis, M.2
  • 5
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L, Jernigan RL, Covell DG. A role for surface hydrophobicity in protein-protein recognition. Prot Sci 1994;3:717-729.
    • (1994) Prot Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 6
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 7
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to α-helix dipoles
    • Warwicker J, Watson HC. Calculation of the electric potential in the active site cleft due to α-helix dipoles. J Mol Biol 1982;157:671-679.
    • (1982) J Mol Biol , vol.157 , pp. 671-679
    • Warwicker, J.1    Watson, H.C.2
  • 8
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson MK, Honig BH. Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis. Proteins 1988;4:7-18.
    • (1988) Proteins , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.H.2
  • 9
    • 0025197061 scopus 로고
    • a's of ionizable groups in proteins: Atomic detail from a continuum electrostatic model
    • a's 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
  • 10
    • 0026124585 scopus 로고
    • Electrostatics and diffusion of molecules in solution: Simulations with the University of Houston Brownian dynamics program
    • Davis ME, Madura JD, Luty BA, McCammon JA. Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian dynamics program. Comp Phys Comm 1991;62:187-197.
    • (1991) Comp Phys Comm , vol.62 , pp. 187-197
    • Davis, M.E.1    Madura, J.D.2    Luty, B.A.3    McCammon, J.A.4
  • 11
    • 0033214412 scopus 로고    scopus 로고
    • Exhaustive docking of molecular fragments on protein binding sites with electrostatic solvation
    • Majeux N, Scarsi M, Apostolakis J, Ehrhard C, Caflisch A. Exhaustive docking of molecular fragments on protein binding sites with electrostatic solvation. Proteins 1999;37:88-105.
    • (1999) Proteins , vol.37 , pp. 88-105
    • Majeux, N.1    Scarsi, M.2    Apostolakis, J.3    Ehrhard, C.4    Caflisch, A.5
  • 12
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 14
    • 84986492566 scopus 로고
    • On the use of conformationally dependent geometry trends from ab initio dipeptide studies to refine potentials for the empirical force field CHARMM
    • Momany FA, Klimkowski VJ, Schäfer L. On the use of conformationally dependent geometry trends from ab initio dipeptide studies to refine potentials for the empirical force field CHARMM. J Comput Chem 1990;11:654-662.
    • (1990) J Comput Chem , vol.11 , pp. 654-662
    • Momany, F.A.1    Klimkowski, V.J.2    Schäfer, L.3
  • 15
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interactions
    • Privalov PL, Gill SG. Stability of protein structure and hydrophobic interactions. Adv Prot Chem 1988;39:191-234.
    • (1988) Adv Prot Chem , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.G.2
  • 16
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Privalov PL, Gill SG. Common features of protein unfolding and dissolution of hydrophobic compounds. Adv Prot Chem 1990;247: 559-561.
    • (1990) Adv Prot Chem , vol.247 , pp. 559-561
    • Privalov, P.L.1    Gill, S.G.2
  • 17
    • 2442481562 scopus 로고
    • Stability of folded conformations
    • Creighton TE. Stability of folded conformations. Curr Opin Struct Biol 1991;1:5-16.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 5-16
    • Creighton, T.E.1
  • 18
    • 0029118487 scopus 로고
    • A free energy analysis of nucleic acid base stacking in aqueous solution
    • Friedman RA, Honig B. A free energy analysis of nucleic acid base stacking in aqueous solution. Biophys J 1995;69:1528-1535.
    • (1995) Biophys J , vol.69 , pp. 1528-1535
    • Friedman, R.A.1    Honig, B.2
  • 19
    • 0001246354 scopus 로고    scopus 로고
    • Docking by Monte Carlo minimization with a solvation correction: Application to an FKBP-substrate complex
    • Caflisch A, Fischer S, Karplus M. Docking by Monte Carlo minimization with a solvation correction: application to an FKBP-substrate complex. J Comput Chem 1997;18:723-743.
    • (1997) J Comput Chem , vol.18 , pp. 723-743
    • Caflisch, A.1    Fischer, S.2    Karplus, M.3
  • 20
    • 0031872292 scopus 로고    scopus 로고
    • Discrimination between native and intentionally misfolded conformations of proteins: ES/IS, a new method for calculating conformational free energy that uses both dynamics simulations with an explicit solvent and an implicit solvent continuum model
    • Vorobjev YN, Almagro JC, Hermans J. Discrimination between native and intentionally misfolded conformations of proteins: ES/IS, a new method for calculating conformational free energy that uses both dynamics simulations with an explicit solvent and an implicit solvent continuum model. Proteins 1998;32:399-413.
    • (1998) Proteins , vol.32 , pp. 399-413
    • Vorobjev, Y.N.1    Almagro, J.C.2    Hermans, J.3
  • 21
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still WC, Tempczyk A, Hawley RC, Hendrickson T. Semianalytical treatment of solvation for molecular mechanics and dynamics. J Am Chem Soc 1990;112:6127-6129.
    • (1990) J Am Chem Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 22
    • 0002636134 scopus 로고
    • Pairwise solute descreening of solute charges from a dielectric medium
    • Hawking GD, Cramer CJ, Trulhar DG. Pairwise solute descreening of solute charges from a dielectric medium. Chem Phys Lett 1995;246:122-129.
    • (1995) Chem Phys Lett , vol.246 , pp. 122-129
    • Hawking, G.D.1    Cramer, C.J.2    Trulhar, D.G.3
  • 23
    • 33748390341 scopus 로고    scopus 로고
    • Parameterized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium
    • Hawkins GD, Cramer CJ, Trulhar DG. Parameterized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium. J Phys Chem 1996;100:19824-19839.
    • (1996) J Phys Chem , vol.100 , pp. 19824-19839
    • Hawkins, G.D.1    Cramer, C.J.2    Trulhar, D.G.3
  • 24
    • 0012227656 scopus 로고    scopus 로고
    • A comprehensive analytical treatment of continuum electrostatics
    • Schaefer M, Karplus M. A comprehensive analytical treatment of continuum electrostatics. J Phys Chem 1996;100:1578-1599.
    • (1996) J Phys Chem , vol.100 , pp. 1578-1599
    • Schaefer, M.1    Karplus, M.2
  • 25
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii
    • Qiu DI, Shenkin PS, Hollinger FP, Still WC. The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii. J Phys Chem A 1997;101: 3005-3014.
    • (1997) J Phys Chem A , vol.101 , pp. 3005-3014
    • Qiu, D.I.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 26
    • 0031248940 scopus 로고    scopus 로고
    • Continuum electrostatic energies of macromolecules in aqueous solutions
    • Scarsi M, Apostolakis J, Caflisch A. Continuum electrostatic energies of macromolecules in aqueous solutions. J Phys Chem A 1997;101:8098-8106.
    • (1997) J Phys Chem A , vol.101 , pp. 8098-8106
    • Scarsi, M.1    Apostolakis, J.2    Caflisch, A.3
  • 27
    • 11644251375 scopus 로고    scopus 로고
    • Comparison of a GB solvation model with explicit solvent simulations: Potentials of mean force and conformational preferences of alanine dipeptide and 1,2-dichloroethane
    • Scarsi M, Apostolakis J, Caflisch A. Comparison of a GB solvation model with explicit solvent simulations: potentials of mean force and conformational preferences of alanine dipeptide and 1,2-dichloroethane. J Phys Chem B 1998;102:3637-3641.
    • (1998) J Phys Chem B , vol.102 , pp. 3637-3641
    • Scarsi, M.1    Apostolakis, J.2    Caflisch, A.3
  • 29
    • 0031358503 scopus 로고    scopus 로고
    • Dielectric screening treatment of electrostatic solvation
    • Luo R, Moult J, Gilson MK. Dielectric screening treatment of electrostatic solvation. J Phys Chem B 1997;101:11226-11236.
    • (1997) J Phys Chem B , vol.101 , pp. 11226-11236
    • Luo, R.1    Moult, J.2    Gilson, M.K.3
  • 30
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein structure
    • Richards FM. Areas, volumes, packing, and protein structure. Ann Rev Biophys Bioeng 1977;6:151-176.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 31
    • 0028143534 scopus 로고
    • Design and synthesis of potent and highly selective thrombin inhibitors
    • Hilpert K, Ackermann J, Banner DW et al. Design and synthesis of potent and highly selective thrombin inhibitors. J Med Chem 1994;37:3889-3901.
    • (1994) J Med Chem , vol.37 , pp. 3889-3901
    • Hilpert, K.1    Ackermann, J.2    Banner, D.W.3
  • 32
    • 0024431034 scopus 로고
    • The refined 1.9-Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9-Å crystal structure of human α-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J 1989;8:3467-3475.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 33
    • 0025837452 scopus 로고
    • Crystallographic analysis at 3.0-Å resolution of the binding to human thrombin of four active site-directed inhibitors
    • Banner DW, Hadvary P. Crystallographic analysis at 3.0-Å resolution of the binding to human thrombin of four active site-directed inhibitors. J Biol Chem 1991;266:20085-20093.
    • (1991) J Biol Chem , vol.266 , pp. 20085-20093
    • Banner, D.W.1    Hadvary, P.2
  • 34
    • 0000437776 scopus 로고
    • Design neuartiger, nichtpeptidischer thrombin-inhibotoren und struktur eines thrombin-inhibitoren-komplexes
    • Obst U, Gramlich V, Diederich F, Weber L, Banner DW. Design neuartiger, nichtpeptidischer Thrombin-Inhibotoren und Struktur eines Thrombin-Inhibitoren-Komplexes. Angew Chem 1995; 107:1874-1877.
    • (1995) Angew Chem , vol.107 , pp. 1874-1877
    • Obst, U.1    Gramlich, V.2    Diederich, F.3    Weber, L.4    Banner, D.W.5
  • 35
    • 0029099770 scopus 로고
    • Crystallographic structure of a peptidyl keto acid inhibitor and human α-thrombin
    • Håkansson K, Tulinsky A, Abelman MM, et al. Crystallographic structure of a peptidyl keto acid inhibitor and human α-thrombin. Bioorgan Med Chem 1995;3:1009-1017.
    • (1995) Bioorgan Med Chem , vol.3 , pp. 1009-1017
    • Håkansson, K.1    Tulinsky, A.2    Abelman, M.M.3
  • 36
    • 0026465007 scopus 로고
    • Refined 2.3 Å x-ray structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA
    • Brandstetter H, Turk D, Hoeffken HW, et al. Refined 2.3 Å x-ray structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. J Mol Biol 1992;226:1085-1099.
    • (1992) J Mol Biol , vol.226 , pp. 1085-1099
    • Brandstetter, H.1    Turk, D.2    Hoeffken, H.W.3
  • 37
    • 0029613291 scopus 로고
    • Farnesyltransferase inhibitors: The successes and surprises of a new class of potential cancer chemotherapeutics
    • Buss JE, Marsters JC. Farnesyltransferase inhibitors: The successes and surprises of a new class of potential cancer chemotherapeutics. Chem Biol 1995;2:787-791.
    • (1995) Chem Biol , vol.2 , pp. 787-791
    • Buss, J.E.1    Marsters, J.C.2
  • 39
    • 0030962347 scopus 로고    scopus 로고
    • The potential of farnesyltransferase inhibitors as cancer chemotherapeutics
    • Gibbs JB, Oliff A. The potential of farnesyltransferase inhibitors as cancer chemotherapeutics. Ann Rev Pharmacol Toxicol 1997;37: 143-166.
    • (1997) Ann Rev Pharmacol Toxicol , vol.37 , pp. 143-166
    • Gibbs, J.B.1    Oliff, A.2
  • 40
    • 0032493317 scopus 로고    scopus 로고
    • Cocrystal structure of protein farnesyltransferase complexed with a diphosphate substrate
    • Long SB, Casey PJ. Beese LS. Cocrystal structure of protein farnesyltransferase complexed with a diphosphate substrate. Biochemistry 1998;37:9612-9618.
    • (1998) Biochemistry , vol.37 , pp. 9612-9618
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 41
    • 0026649648 scopus 로고
    • The MDM-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand J, Zambetti GP, Olson DC, George D, Levine AJ. The MDM-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 1992;69:1237.
    • (1992) Cell , vol.69 , pp. 1237
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 42
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Russie PH, Gorina S, Marechal V, et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996;274:948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Russie, P.H.1    Gorina, S.2    Marechal, V.3
  • 44
    • 0026504525 scopus 로고
    • Homeobox genes and axial patterning
    • McGinnis W, Krumlauf R. Homeobox genes and axial patterning. Cell 1992;68:283-302.
    • (1992) Cell , vol.68 , pp. 283-302
    • McGinnis, W.1    Krumlauf, R.2
  • 45
    • 0033582545 scopus 로고    scopus 로고
    • Structure of a HoxB1-Pbx1 heterodimer bound to DNA: Role of the hexapeptide and a fourth homeodomain helix in complex formation
    • Piper DE, Batchelor AH, Chang CP, Cleary ML, Wolberger C. Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation. Cell 1999;96:587-597.
    • (1999) Cell , vol.96 , pp. 587-597
    • Piper, D.E.1    Batchelor, A.H.2    Chang, C.P.3    Cleary, M.L.4    Wolberger, C.5
  • 47
    • 0022157945 scopus 로고
    • The regulatory chain of the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the s-100 protein of glial cells
    • Gerke V, Weber K. The regulatory chain of the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the s-100 protein of glial cells. EMBO J 1985;4:2917-2910.
    • (1985) EMBO J , vol.4 , pp. 2917-12910
    • Gerke, V.1    Weber, K.2
  • 48
    • 0028844290 scopus 로고
    • Annexin II tetramer:Structure and function
    • Waisman DM. Annexin II tetramer:structure and function. Mol Cell Biochem 1995;149/150:301-322.
    • (1995) Mol Cell Biochem , vol.149-150 , pp. 301-322
    • Waisman, D.M.1
  • 49
    • 0030998465 scopus 로고    scopus 로고
    • Annexins and membrane dynamics
    • Gerke V, Moss S. Annexins and membrane dynamics. Biochim Biophys Acta 1997;1357:129-154.
    • (1997) Biochim Biophys Acta , vol.1357 , pp. 129-154
    • Gerke, V.1    Moss, S.2
  • 51
    • 0032924354 scopus 로고    scopus 로고
    • Crystal structure of a complex of p11, the ligand of annexin II, with the annexin II N-terminal peptide
    • Rety S, Sopkova J, Renouard M, et al. Crystal structure of a complex of p11, the ligand of annexin II, with the annexin II N-terminal peptide. Nature Struct Biol 1999;6:89-95.
    • (1999) Nature Struct Biol , vol.6 , pp. 89-95
    • Rety, S.1    Sopkova, J.2    Renouard, M.3
  • 53
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea EK, Rutkowski R, Kim PS. Evidence that the leucine zipper is a coiled coil. Science 1989;243:538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 54
    • 0027299695 scopus 로고
    • Three-dimensional structure of an anti-steroid Fab' and progesterone-Fab' complex
    • Arevalo JH, Stura EA, Taussig MJ, Wilson IA. Three-dimensional structure of an anti-steroid Fab' and progesterone-Fab' complex. J Mol Biol 1993;231:103-118.
    • (1993) J Mol Biol , vol.231 , pp. 103-118
    • Arevalo, J.H.1    Stura, E.A.2    Taussig, M.J.3    Wilson, I.A.4
  • 55
    • 0033214756 scopus 로고    scopus 로고
    • Insight into odorant perception: The crystal structure and binding characteristics of antibody fragments against the musk odorant traseolide
    • in press
    • Langedijk AC, Spinelli S, Anguille C, et al. Insight into odorant perception: the crystal structure and binding characteristics of antibody fragments against the musk odorant traseolide. J Mol Biol 1999:in press.
    • (1999) J Mol Biol
    • Langedijk, A.C.1    Spinelli, S.2    Anguille, C.3
  • 56
    • 0031568813 scopus 로고    scopus 로고
    • A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex
    • Mittl PRE, Di Marco S, Fendrich G, et al. A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex. Structure 1996;5:253-264.
    • (1996) Structure , vol.5 , pp. 253-264
    • Mittl, P.R.E.1    Di Marco, S.2    Fendrich, G.3
  • 57
    • 0025108755 scopus 로고
    • Crystallographic analysis of a complex between human immunodeficiency virus type 1 and acetyl-pepstatin at 2.0 Åresolution
    • Fitzgerald PMD, McKeever BM, VanMiddlesworth JF, et al. Crystallographic analysis of a complex between human immunodeficiency virus type 1 and acetyl-pepstatin at 2.0 Åresolution. J Biol Chem 1990;265:14209-14219.
    • (1990) J Biol Chem , vol.265 , pp. 14209-14219
    • Fitzgerald, P.M.D.1    McKeever, B.M.2    VanMiddlesworth, J.F.3
  • 58
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sánchez R, Šali A. Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc Natl Acad Sci USA 1998; 95:13597-13602.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13597-13602
    • Sánchez, R.1    Šali, A.2
  • 59
    • 84988141840 scopus 로고
    • Solving the finite difference linearized Poisson-Boltzmann equation: A comparison of relaxation and conjugate gradient methods
    • Davis ME, McCammon JA. Solving the finite difference linearized Poisson-Boltzmann equation: a comparison of relaxation and conjugate gradient methods. J Comput Chem 1989;10:386-391.
    • (1989) J Comput Chem , vol.10 , pp. 386-391
    • Davis, M.E.1    McCammon, J.A.2
  • 60
    • 84986524546 scopus 로고
    • Calculating electrostatic forces from grid-calculated potentials
    • Davis ME, McCammon JA. Calculating electrostatic forces from grid-calculated potentials. J Comput Chem 1990;11:401-409.
    • (1990) J Comput Chem , vol.11 , pp. 401-409
    • Davis, M.E.1    McCammon, J.A.2
  • 61
    • 84986522972 scopus 로고
    • Dielectric boundary smoothing in finite difference solutions of the poisson equation: An approach to improve accuracy and convergence
    • Davis ME, McCammon JA. Dielectric boundary smoothing in finite difference solutions of the Poisson equation: An approach to improve accuracy and convergence. J Comput Chem 1991;12:909-912.
    • (1991) J Comput Chem , vol.12 , pp. 909-912
    • Davis, M.E.1    McCammon, J.A.2


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