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Volumn 52, Issue 4, 2003, Pages 492-509

Discrimination of native loop conformations in membrane proteins: Decoy library design and evaluation of effective energy scoring functions

Author keywords

B factor; Effective energy function; Implicit solvent; Loop prediction; Membrane protein; Protein structure prediction

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); GLOBULAR PROTEIN; MEMBRANE PROTEIN; RHODOPSIN;

EID: 0041919601     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10404     Document Type: Article
Times cited : (24)

References (63)
  • 2
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R. X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 2002;415:287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 3
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 2000;405:647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 5
    • 0029902780 scopus 로고    scopus 로고
    • Bridging the protein sequence-structure gap by structure predictions
    • Rost B, Sander C. Bridging the protein sequence-structure gap by structure predictions. Annu Rev Biophys Biomolec Struct 1996;25:113-136.
    • (1996) Annu Rev Biophys Biomolec Struct , vol.25 , pp. 113-136
    • Rost, B.1    Sander, C.2
  • 6
    • 0042624145 scopus 로고    scopus 로고
    • Comparative protein structure modeling in genomics
    • Sanchez R, Sali A. Comparative protein structure modeling in genomics. J Comput Phys 1999;151:388-401.
    • (1999) J Comput Phys , vol.151 , pp. 388-401
    • Sanchez, R.1    Sali, A.2
  • 7
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin JM. The probable arrangement of the helices in G protein-coupled receptors. EMBO J 1993;12:1693-1703.
    • (1993) EMBO J , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 8
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros JA, Shi L, Javitch JA. Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol Pharmacol 2001;60:1-19.
    • (2001) Mol Pharmacol , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 9
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled structures and mechanisms
    • Visiers I, Ballesteros JA, Weinstein H. Three-dimensional representations of G protein-coupled structures and mechanisms. Methods Enzymol 2002;343:329-371.
    • (2002) Methods Enzymol , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 10
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism - An overview
    • Higgins CF. ABC transporters: Physiology, structure and mechanism - an overview. Res Microbiol 2001;152:205-210.
    • (2001) Res Microbiol , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 11
    • 0037307081 scopus 로고    scopus 로고
    • Molecular modeling of ion channels: Structural predictions
    • Giorgetti A, Carloni P. Molecular modeling of ion channels: structural predictions. Curr Opin Chem Biol 2003;7:150-156.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 150-156
    • Giorgetti, A.1    Carloni, P.2
  • 12
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, Lesk AM. The relation between the divergence of sequence and structure in proteins. EMBO J 1986;5:823-826.
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 13
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction
    • Xiang Z, Soto C, Honig B. Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. Proc Natl Acad Sci USA 2002;99:7432-7437.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.2    Honig, B.3
  • 14
    • 0031564640 scopus 로고    scopus 로고
    • PDB-based protein loop prediction: Parameters for selection and methods for optimization
    • van Vlijmen HWT, Karplus M. PDB-based protein loop prediction: Parameters for selection and methods for optimization. J Mol Biol 1997;267:975-1001.
    • (1997) J Mol Biol , vol.267 , pp. 975-1001
    • Van Vlijmen, H.W.T.1    Karplus, M.2
  • 15
    • 0034031680 scopus 로고    scopus 로고
    • Effective energy functions for protein structure prediction
    • Lazaridis T, Karplus M. Effective energy functions for protein structure prediction. Curr Opin Struct Biol 2000;10:139-145.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 139-145
    • Lazaridis, T.1    Karplus, M.2
  • 16
    • 0037079585 scopus 로고    scopus 로고
    • Identifying native-like protein structures using physics-based potentials
    • Dominy BN, Brooks CL. Identifying native-like protein structures using physics-based potentials. J Comput Chem 2002;23:147-160.
    • (2002) J Comput Chem , vol.23 , pp. 147-160
    • Dominy, B.N.1    Brooks, C.L.2
  • 17
    • 0033531959 scopus 로고    scopus 로고
    • Discrimination of the native from misfolded protein models with an energy function including implicit solvation
    • Lazaridis T, Karplus M. Discrimination of the native from misfolded protein models with an energy function including implicit solvation. J Mol Biol 1999;288:477-487.
    • (1999) J Mol Biol , vol.288 , pp. 477-487
    • Lazaridis, T.1    Karplus, M.2
  • 18
    • 0029077858 scopus 로고
    • A new computational model for protein folding based on atomic solvation
    • Wang YH, Zhang H, Scott RA. A new computational model for protein folding based on atomic solvation. Prot Sci 1995;4:1402-1411.
    • (1995) Prot Sci , vol.4 , pp. 1402-1411
    • Wang, Y.H.1    Zhang, H.2    Scott, R.A.3
  • 19
    • 0036533445 scopus 로고    scopus 로고
    • A critical analysis of continuum electrostatics: The screen coulomb potential-implicit solvent model and the study of the alanine dipeptide and discrimination of misfolded structures of proteins
    • Hassan SA, Mehler EL. A critical analysis of continuum electrostatics: The screen coulomb potential-implicit solvent model and the study of the alanine dipeptide and discrimination of misfolded structures of proteins. Proteins 2002;47:45-61.
    • (2002) Proteins , vol.47 , pp. 45-61
    • Hassan, S.A.1    Mehler, E.L.2
  • 20
    • 0042139644 scopus 로고    scopus 로고
    • Comparison of generalized Born and Poisson models: Energetics and dynamics of HIV protease
    • David L, Luo R, Gilson MK. Comparison of generalized Born and Poisson models: Energetics and dynamics of HIV protease. J Comput Chem 2000;21:295-309.
    • (2000) J Comput Chem , vol.21 , pp. 295-309
    • David, L.1    Luo, R.2    Gilson, M.K.3
  • 21
    • 0031075977 scopus 로고    scopus 로고
    • Solvation free energies of peptides: Comparison of approximate continuum solvation models with accurate solution of the Poisson-Boltzmann equation
    • Edinger SR, Cortis C, Shenkin PS, Friesner RA. Solvation free energies of peptides: Comparison of approximate continuum solvation models with accurate solution of the Poisson-Boltzmann equation. J Phys Chem B 1997;101:1190-1197.
    • (1997) J Phys Chem B , vol.101 , pp. 1190-1197
    • Edinger, S.R.1    Cortis, C.2    Shenkin, P.S.3    Friesner, R.A.4
  • 22
    • 0036836611 scopus 로고    scopus 로고
    • Evaluating CASP4 predictions with physical energy functions
    • Feig M, Brooks CL. Evaluating CASP4 predictions with physical energy functions. Proteins 2002;49:232-245.
    • (2002) Proteins , vol.49 , pp. 232-245
    • Feig, M.1    Brooks, C.L.2
  • 23
    • 0033152803 scopus 로고    scopus 로고
    • Correlation between knowledge-based and detailed atomic potentials: Application to the unfolding of the GCN4 leucine zipper
    • Mohanty D, Dominy BN, Kolinski A, Brooks CL, Skolnick J. Correlation between knowledge-based and detailed atomic potentials: Application to the unfolding of the GCN4 leucine zipper. Proteins 1999;35:447-452.
    • (1999) Proteins , vol.35 , pp. 447-452
    • Mohanty, D.1    Dominy, B.N.2    Kolinski, A.3    Brooks, C.L.4    Skolnick, J.5
  • 27
    • 0000036869 scopus 로고    scopus 로고
    • Simulations of activation free energies in molecular systems
    • Neria E, Fischer S, Karplus M. Simulations of activation free energies in molecular systems. J Chem Phys 1996;105:1902-1921.
    • (1996) J Chem Phys , vol.105 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 28
    • 0036301334 scopus 로고    scopus 로고
    • Ions and counterions in a biological channel: A molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1M KC1 aqueous salt solution
    • Im W, Roux B. Ions and counterions in a biological channel: A molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1M KC1 aqueous salt solution. J Mol Biol 2002;319:1177-1197.
    • (2002) J Mol Biol , vol.319 , pp. 1177-1197
    • Im, W.1    Roux, B.2
  • 29
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure and thermodynamics
    • R. Prigogine, editor. Wiley: New York
    • Brooks CL, Karplus M, Pettitt BM. Proteins: A theoretical perspective of dynamics, structure and thermodynamics. In: R. Prigogine, editor. Advances in chemical physics. Wiley: New York; 1988.
    • (1988) Advances in Chemical Physics
    • Brooks, C.L.1    Karplus, M.2    Pettitt, B.M.3
  • 30
    • 0028895567 scopus 로고
    • Discriminating compact nonnative structures from the native structure of globular proteins
    • Wang YH, Zhang H, Li W, Scott RA. Discriminating compact nonnative structures from the native structure of globular proteins. Proc Natl Acad Sci U S A 1995;92:709-713.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 709-713
    • Wang, Y.H.1    Zhang, H.2    Li, W.3    Scott, R.A.4
  • 31
    • 0029831680 scopus 로고    scopus 로고
    • An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies
    • Kelley LA, Gardner SP, Sutcliffe MJ. An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies. Protein Eng 1996;9:1063-1065.
    • (1996) Protein Eng , vol.9 , pp. 1063-1065
    • Kelley, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 32
    • 0033853177 scopus 로고    scopus 로고
    • Decoys 'R' Us: A database of incorrect conformations to improve protein structure prediction
    • Samudrala R, Levitt M. Decoys 'R' Us: A database of incorrect conformations to improve protein structure prediction. Prot Sci 2000;9:1399-1401.
    • (2000) Prot Sci , vol.9 , pp. 1399-1401
    • Samudrala, R.1    Levitt, M.2
  • 33
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson L, Eisenberg D. Atomic solvation parameters applied to molecular dynamics of proteins in solution. Prot Sci 1992;1:227-235.
    • (1992) Prot Sci , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 34
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D, McLachlan AD. Solvation energy in protein folding and binding. Nature 1986;319:199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 35
    • 0035874147 scopus 로고    scopus 로고
    • Optimization of solvation models for predicting the structure of surface loops in proteins
    • Das B, Meirovitch H. Optimization of solvation models for predicting the structure of surface loops in proteins. Proteins 2001;43:303-314.
    • (2001) Proteins , vol.43 , pp. 303-314
    • Das, B.1    Meirovitch, H.2
  • 36
    • 0000152788 scopus 로고
    • Interpretation of protein folding and binding with atomic solvation parameters
    • Eisenberg D, Wesson L, Yamashita M. Interpretation of protein folding and binding with atomic solvation parameters. Chem Scrip 1989;29A:217-221.
    • (1989) Chem Scrip , vol.29 A , pp. 217-221
    • Eisenberg, D.1    Wesson, L.2    Yamashita, M.3
  • 37
    • 0028818570 scopus 로고
    • Comparison of atomic solvation parametric sets: Applicability and limitations in protein folding and binding
    • Juffer AH, Eisenhaber F, Hubbard SJ, Walther D, Argos P. Comparison of atomic solvation parametric sets: Applicability and limitations in protein folding and binding. Prot Sci 1995;4:2499-2509.
    • (1995) Prot Sci , vol.4 , pp. 2499-2509
    • Juffer, A.H.1    Eisenhaber, F.2    Hubbard, S.J.3    Walther, D.4    Argos, P.5
  • 38
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis T, Karplus M. Effective energy function for proteins in solution. Proteins 1999;35:133-152.
    • (1999) Proteins , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 39
    • 0032484151 scopus 로고    scopus 로고
    • Solution conformations and thermodynamics of structured peptides: Molecular dynamics simulation with an implicit solvation model
    • Schaefer M, Bartels C, Karplus M. Solution conformations and thermodynamics of structured peptides: Molecular dynamics simulation with an implicit solvation model. J Mol Biol 1998;284:835-848.
    • (1998) J Mol Biol , vol.284 , pp. 835-848
    • Schaefer, M.1    Bartels, C.2    Karplus, M.3
  • 40
    • 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
  • 41
    • 0035976325 scopus 로고    scopus 로고
    • Effective atom volumes for implicit solvent models: Comparison between voronoi volumes and minimum fluctuation volumes
    • Schaefer M, Bartels C, LeClerc F, Karplus M. Effective atom volumes for implicit solvent models: Comparison between voronoi volumes and minimum fluctuation volumes. J Comp Chem 2001; 22:1857-1879.
    • (2001) J Comp Chem , vol.22 , pp. 1857-1879
    • Schaefer, M.1    Bartels, C.2    LeClerc, F.3    Karplus, M.4
  • 42
    • 0031167555 scopus 로고    scopus 로고
    • Atomic radii for continuum electrostatics calculations based on molecular dynamics free energy simulations
    • Nina M, Beglov D, Roux B. Atomic radii for continuum electrostatics calculations based on molecular dynamics free energy simulations. J Phys Chem 1997;101:5239-5248.
    • (1997) J Phys Chem , vol.101 , pp. 5239-5248
    • Nina, M.1    Beglov, D.2    Roux, B.3
  • 43
    • 0029871791 scopus 로고    scopus 로고
    • Using a hydrophobic contact potential to evaluate native and near-native folds generated by molecular dynamics simulations
    • Huang ES, Subbiah S, Tsai J, Levitt M. Using a hydrophobic contact potential to evaluate native and near-native folds generated by molecular dynamics simulations. J Mol Biol 1996;257:716-725.
    • (1996) J Mol Biol , vol.257 , pp. 716-725
    • Huang, E.S.1    Subbiah, S.2    Tsai, J.3    Levitt, M.4
  • 44
    • 0031557390 scopus 로고    scopus 로고
    • Factors affecting the ability of energy functions to discriminate correct from incorrect folds
    • Park BH, Huang ES, Levitt M. Factors affecting the ability of energy functions to discriminate correct from incorrect folds. J Mol Biol 1997;266:831-846.
    • (1997) J Mol Biol , vol.266 , pp. 831-846
    • Park, B.H.1    Huang, E.S.2    Levitt, M.3
  • 45
    • 0034486196 scopus 로고    scopus 로고
    • Free energy determinants of tertiary structure and the evaluation of protein models
    • Petrey D, Honig B. Free energy determinants of tertiary structure and the evaluation of protein models. Protein Sci 2000;9:2181-2191.
    • (2000) Protein Sci , vol.9 , pp. 2181-2191
    • Petrey, D.1    Honig, B.2
  • 46
    • 0035703311 scopus 로고    scopus 로고
    • Analysis and assessment of comparative modeling predictions in CASP4
    • Tramontano A, Leplae R, Morea V. Analysis and assessment of comparative modeling predictions in CASP4. Proteins 2001;Suppl 5:22-38.
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 22-38
    • Tramontano, A.1    Leplae, R.2    Morea, V.3
  • 47
    • 0028040064 scopus 로고
    • Evaluation of the conformational free energies of loops in proteins
    • Smith KC, Honig B. Evaluation of the conformational free energies of loops in proteins. Proteins 1994;18:119-132.
    • (1994) Proteins , vol.18 , pp. 119-132
    • Smith, K.C.1    Honig, B.2
  • 48
    • 0033654297 scopus 로고    scopus 로고
    • Generalized born models of macromolecular solvation effects
    • Bashford D, Case DA. Generalized born models of macromolecular solvation effects. Annu Rev Phys Chem 2000;51:129-152.
    • (2000) Annu Rev Phys Chem , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.A.2
  • 49
    • 0036283048 scopus 로고    scopus 로고
    • Evolution and physics in comparative protein structure modeling
    • Fiser A, Feig M, Brooks CL, Sali A. Evolution and physics in comparative protein structure modeling. Acc Chem Res 2002;35:413-421.
    • (2002) Acc Chem Res , vol.35 , pp. 413-421
    • Fiser, A.1    Feig, M.2    Brooks, C.L.3    Sali, A.4
  • 50
    • 0035882571 scopus 로고    scopus 로고
    • Influence of rotational energy barriers to the conformational search of protein loops in molecular dynamics and ranking the conformations
    • Tappura K. Influence of rotational energy barriers to the conformational search of protein loops in molecular dynamics and ranking the conformations. Proteins 2001;44:167-179.
    • (2001) Proteins , vol.44 , pp. 167-179
    • Tappura, K.1
  • 51
    • 0037093647 scopus 로고    scopus 로고
    • Positioning of anchor groups in protein loop prediction: The importance of solvent accessibility and secondary structure elements
    • Wohlfahrt G, Hangoc V, Schomburg D. Positioning of anchor groups in protein loop prediction: The importance of solvent accessibility and secondary structure elements. Proteins 2002;47:370-378.
    • (2002) Proteins , vol.47 , pp. 370-378
    • Wohlfahrt, G.1    Hangoc, V.2    Schomburg, D.3
  • 52
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RKG, Sali A. Modeling of loops in protein structures. Protein Sci 2000;9:1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.G.2    Sali, A.3
  • 53
    • 0033135619 scopus 로고    scopus 로고
    • Prediction of loop geometries using a generalized born model of solvation effects
    • Rapp CS, Friesner RA. Prediction of loop geometries using a generalized born model of solvation effects. Proteins 1999;35:173-183.
    • (1999) Proteins , vol.35 , pp. 173-183
    • Rapp, C.S.1    Friesner, R.A.2
  • 54
    • 0001444020 scopus 로고    scopus 로고
    • Implicit solvent models: Combining an analytical formulation of continuum electrostatics with simple models of the hydrophobic effect
    • Wagner F, Simonson T. Implicit solvent models: Combining an analytical formulation of continuum electrostatics with simple models of the hydrophobic effect. J Comput Chem 1999;20:322-335.
    • (1999) J Comput Chem , vol.20 , pp. 322-335
    • Wagner, F.1    Simonson, T.2
  • 55
    • 0034560338 scopus 로고    scopus 로고
    • Discrimination of near-native protein structures from misfolded models by empirical free energy functions
    • Gatchell DW, Dennis S, Vajda S. Discrimination of near-native protein structures from misfolded models by empirical free energy functions. Proteins 2000;41:518-534.
    • (2000) Proteins , vol.41 , pp. 518-534
    • Gatchell, D.W.1    Dennis, S.2    Vajda, S.3
  • 56
    • 0032461411 scopus 로고    scopus 로고
    • Selecting near-native conformations in homology modeling: The role of molecular mechanics and solvation terms
    • Janardhan A, Vajda S. Selecting near-native conformations in homology modeling: The role of molecular mechanics and solvation terms. Protein Sci 1998;7:1772-1780.
    • (1998) Protein Sci , vol.7 , pp. 1772-1780
    • Janardhan, A.1    Vajda, S.2
  • 57
    • 0037194983 scopus 로고    scopus 로고
    • Introducing an implicit membrane in generalized Born/solvent accessibility continuum solvent models
    • Spassov VZ, Yan K, Szalma S. Introducing an implicit membrane in generalized Born/solvent accessibility continuum solvent models. J Phys Chem B 2002;106:8726-8738.
    • (2002) J Phys Chem B , vol.106 , pp. 8726-8738
    • Spassov, V.Z.1    Yan, K.2    Szalma, S.3
  • 58
    • 0034333207 scopus 로고    scopus 로고
    • Dipole lattice membrane model for protein calculations
    • Grossfield A, Sachs J, Woolf TB. Dipole lattice membrane model for protein calculations. Proteins 2002;41:211-223.
    • (2002) Proteins , vol.41 , pp. 211-223
    • Grossfield, A.1    Sachs, J.2    Woolf, T.B.3
  • 59
    • 0033468737 scopus 로고    scopus 로고
    • Application of a pairwise generalized Born model to proteins and nucleic acids: Inclusion of salt effects
    • Srinivasan J, Trevathan MW, Beroza P, Case DA. Application of a pairwise generalized Born model to proteins and nucleic acids: Inclusion of salt effects. Theor Chem Acc 1999;101:426-434.
    • (1999) Theor Chem Acc , vol.101 , pp. 426-434
    • Srinivasan, J.1    Trevathan, M.W.2    Beroza, P.3    Case, D.A.4
  • 60
    • 0002636134 scopus 로고
    • Pairwise solute descreening of solute charges from a dielectric medium
    • Hawkins GD, Cramer CJ, Truhlar 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
    • Hawkins, G.D.1    Cramer, C.J.2    Truhlar, D.G.3
  • 61
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation: A fast analytical method for the calculation of approximate Born radii
    • Qiu D, 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.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 62
    • 84961985307 scopus 로고    scopus 로고
    • Development of a generalized Born model parametrization for proteins and nucleic acids
    • Dominy BN, Brooks CL. Development of a generalized Born model parametrization for proteins and nucleic acids. J Phys Chem B 1999;103:3765-3773.
    • (1999) J Phys Chem B , vol.103 , pp. 3765-3773
    • Dominy, B.N.1    Brooks, C.L.2
  • 63
    • 0001246294 scopus 로고    scopus 로고
    • Generalized Born model based on a surface integral formulation
    • Ghosh A, Rapp CS, Friesner RA. Generalized Born model based on a surface integral formulation. J Phys Chem B 1998;102:10983-10990.
    • (1998) J Phys Chem B , vol.102 , pp. 10983-10990
    • Ghosh, A.1    Rapp, C.S.2    Friesner, R.A.3


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