메뉴 건너뛰기




Volumn 79, Issue 12, 2011, Pages 3448-3468

Computational protein design with a generalized born solvent model: Application to asparaginyl-tRNA synthetase

Author keywords

Aminoacyl tRNA synthetases; Asparaginyl tRNA synthetase; Computational protein design; Generalized Born model; Genetic code; Implicit solvent models; Molecular dynamics simulations; Poisson Boltzmann calculations; Protein ligand interactions

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID;

EID: 81055158020     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23042     Document Type: Article
Times cited : (17)

References (137)
  • 2
    • 34548528158 scopus 로고    scopus 로고
    • Progress in computational protein design
    • Lippow SM, Tidor B. Progress in computational protein design. Curr Opin Biotechn 2007; 18: 305-311.
    • (2007) Curr Opin Biotechn , vol.18 , pp. 305-311
    • Lippow, S.M.1    Tidor, B.2
  • 3
    • 34147169516 scopus 로고    scopus 로고
    • Potential energy functions for protein design
    • Boas FE, Harbury PB. Potential energy functions for protein design. Curr Opin Struct Biol 2007; 17: 199-204.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 199-204
    • Boas, F.E.1    Harbury, P.B.2
  • 4
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modelling with Rosetta
    • Das R, Baker D. Macromolecular modelling with Rosetta. Ann Rev Biochem 2008; 77: 363-382.
    • (2008) Ann Rev Biochem , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 5
    • 70349328238 scopus 로고    scopus 로고
    • Computational protein design as a tool for fold recognition
    • Schmidt am Busch M, Mignon D, Simonson T. Computational protein design as a tool for fold recognition. Proteins 2009; 77: 139-158.
    • (2009) Proteins , vol.77 , pp. 139-158
    • Schmidt am Busch, M.1    Mignon, D.2    Simonson, T.3
  • 6
    • 69249158062 scopus 로고    scopus 로고
    • Computational design of affinity and specificity at protein-protein interfaces
    • Karanicolas J, Kuhlman B. Computational design of affinity and specificity at protein-protein interfaces. Curr Opin Struct Biol 2009; 19: 458-463.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 458-463
    • Karanicolas, J.1    Kuhlman, B.2
  • 7
    • 65349142516 scopus 로고    scopus 로고
    • Computational tools for designing and engineering biocatalysts
    • Dambrovsky J, Brezovsky J. Computational tools for designing and engineering biocatalysts. Curr Opin Chem Biol 2009; 13: 26-34.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 26-34
    • Dambrovsky, J.1    Brezovsky, J.2
  • 8
    • 70349775833 scopus 로고    scopus 로고
    • Backbone flexibility in computational protein design
    • Mandell DJ, Kortemme T. Backbone flexibility in computational protein design. Curr Opin Biotechn 2009; 20: 420-428.
    • (2009) Curr Opin Biotechn , vol.20 , pp. 420-428
    • Mandell, D.J.1    Kortemme, T.2
  • 9
    • 67650397253 scopus 로고    scopus 로고
    • Challenges in the computational design of proteins
    • Suarez M, Jaramillo A. Challenges in the computational design of proteins. J R Soc Interface 2009; 6: 5477-5491.
    • (2009) J R Soc Interface , vol.6 , pp. 5477-5491
    • Suarez, M.1    Jaramillo, A.2
  • 10
    • 77951232176 scopus 로고    scopus 로고
    • Flexible induced-fit backbone refinement in molecular docking
    • Mashiach E, Nussinov R, Wolfson HJ. Flexible induced-fit backbone refinement in molecular docking. Proteins 2009; 78: 1503-1519.
    • (2009) Proteins , vol.78 , pp. 1503-1519
    • Mashiach, E.1    Nussinov, R.2    Wolfson, H.J.3
  • 11
    • 77956280650 scopus 로고    scopus 로고
    • Computational protein design: validation and possible relevance as a tool for homology searching and fold recognition
    • Schmidt am Busch M, Sedano A, Simonson T. Computational protein design: validation and possible relevance as a tool for homology searching and fold recognition. PloS One 2010; 5: e10410.
    • (2010) PloS One , vol.5
    • Schmidt am Busch, M.1    Sedano, A.2    Simonson, T.3
  • 12
    • 75849152422 scopus 로고    scopus 로고
    • Computational protein design: Advances in the design and redesign of biomolecular nanostructures
    • Saven JG. Computational protein design: Advances in the design and redesign of biomolecular nanostructures. Curr Opin Colloid Interf Sci 2010; 15: 13-17.
    • (2010) Curr Opin Colloid Interf Sci , vol.15 , pp. 13-17
    • Saven, J.G.1
  • 13
    • 77950833121 scopus 로고    scopus 로고
    • Computational methods for de novo protein design and its applications to the Human Immunodeficiency Virus 1, Purine Nucleoside Phosphorylase, Ubiquitin Specific Protease 7, and Histone Demethylases
    • Bellows ML, Floudas CA. Computational methods for de novo protein design and its applications to the Human Immunodeficiency Virus 1, Purine Nucleoside Phosphorylase, Ubiquitin Specific Protease 7, and Histone Demethylases. Current drug targets 2010; 11: 264-278.
    • (2010) Current drug targets , vol.11 , pp. 264-278
    • Bellows, M.L.1    Floudas, C.A.2
  • 16
    • 33750058234 scopus 로고    scopus 로고
    • Rational design of new binding specificity by simultaneous mutagenesis of calmodulin and a target peptide
    • Green DF, Dennis AT, Fam PS, Tidor B, Jasanoff A. Rational design of new binding specificity by simultaneous mutagenesis of calmodulin and a target peptide. Biochemistry 2006; 45: 12547-12559.
    • (2006) Biochemistry , vol.45 , pp. 12547-12559
    • Green, D.F.1    Dennis, A.T.2    Fam, P.S.3    Tidor, B.4    Jasanoff, A.5
  • 17
    • 77950578546 scopus 로고    scopus 로고
    • Computational design of protein-ligand binding: modifying the specificity of asparaginyl-tRNA synthetase
    • Lopes A, Schmidt am Busch M, Simonson T. Computational design of protein-ligand binding: modifying the specificity of asparaginyl-tRNA synthetase. J Comp Chem 2010; 31: 1273-1286.
    • (2010) J Comp Chem , vol.31 , pp. 1273-1286
    • Lopes, A.1    Schmidt am Busch, M.2    Simonson, T.3
  • 18
    • 0037699589 scopus 로고    scopus 로고
    • Integrated computational and experimental approach for lead optimization and design of compstatin variants with improved activity
    • Klepeis JL, Floudas CA, Morikis D, Tsokos CG, Argyropoulos E, Spruce L, Lambris JD. Integrated computational and experimental approach for lead optimization and design of compstatin variants with improved activity. J Am Chem Soc 2003; 125: 8422-8423.
    • (2003) J Am Chem Soc , vol.125 , pp. 8422-8423
    • Klepeis, J.L.1    Floudas, C.A.2    Morikis, D.3    Tsokos, C.G.4    Argyropoulos, E.5    Spruce, L.6    Lambris, J.D.7
  • 19
    • 0344392711 scopus 로고    scopus 로고
    • Exploring the origins of binding specificity through the computational redesign of calmodulin
    • Shifman JM, Mayo SL. Exploring the origins of binding specificity through the computational redesign of calmodulin. Proc Natl Acad Sci USA 2003; 100: 13274-13279.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13274-13279
    • Shifman, J.M.1    Mayo, S.L.2
  • 20
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow SM, Wittrup KD, Tidor B. Computational design of antibody-affinity improvement beyond in vivo maturation. Nat Biotechnol 2007; 25: 1171-1176.
    • (2007) Nat Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 21
    • 38549143261 scopus 로고    scopus 로고
    • Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease
    • Altman MD, Nalivaika EA, Prabu-Jeyabalan M, Schiffer CA, Tidor B. Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease. Proteins 2008; 70: 678-694.
    • (2008) Proteins , vol.70 , pp. 678-694
    • Altman, M.D.1    Nalivaika, E.A.2    Prabu-Jeyabalan, M.3    Schiffer, C.A.4    Tidor, B.5
  • 23
    • 61449234107 scopus 로고    scopus 로고
    • Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC
    • Haidar JN, Pierce B, Yu Y, Tong WW, Li M, Weng ZP. Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC. Proteins 2009; 74: 948-960.
    • (2009) Proteins , vol.74 , pp. 948-960
    • Haidar, J.N.1    Pierce, B.2    Yu, Y.3    Tong, W.W.4    Li, M.5    Weng, Z.P.6
  • 26
    • 34547691430 scopus 로고    scopus 로고
    • Full-sequence computational design and solution structure of a thermostable protein variant
    • Shah PS, Hom GK, Ross SA, Lassila JK, Crowhurst KA, Mayo SL. Full-sequence computational design and solution structure of a thermostable protein variant. J Mol Biol 2007; 372: 1-6.
    • (2007) J Mol Biol , vol.372 , pp. 1-6
    • Shah, P.S.1    Hom, G.K.2    Ross, S.A.3    Lassila, J.K.4    Crowhurst, K.A.5    Mayo, S.L.6
  • 28
    • 31944435091 scopus 로고    scopus 로고
    • Computational design of a single aminoacid sequence that can switch between two distinct protein folds
    • Ambroggio XI, Kuhlman B. Computational design of a single aminoacid sequence that can switch between two distinct protein folds. J Am Chem Soc 2006; 128: 1154-1161.
    • (2006) J Am Chem Soc , vol.128 , pp. 1154-1161
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 29
    • 0345304457 scopus 로고    scopus 로고
    • Computational design and characterization of a monomeric helical dinuclear metalloprotein
    • Calhoun JR, Kono H, Lahr S, Wang W, deGrado WF, Saven JG. Computational design and characterization of a monomeric helical dinuclear metalloprotein. J Mol Biol 2003; 334: 1101-1115.
    • (2003) J Mol Biol , vol.334 , pp. 1101-1115
    • Calhoun, J.R.1    Kono, H.2    Lahr, S.3    Wang, W.4    deGrado, W.F.5    Saven, J.G.6
  • 33
    • 0346101759 scopus 로고    scopus 로고
    • Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance channel
    • Chaloupkova R, Sykorova J, Prokop Z, Jesenska A, Monincova M, Pavlova M, Tsuda M, Nagata Y, Dambrovsky J. Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance channel. J Biol Chem 2003; 278: 52622-52628.
    • (2003) J Biol Chem , vol.278 , pp. 52622-52628
    • Chaloupkova, R.1    Sykorova, J.2    Prokop, Z.3    Jesenska, A.4    Monincova, M.5    Pavlova, M.6    Tsuda, M.7    Nagata, Y.8    Dambrovsky, J.9
  • 35
    • 33745927413 scopus 로고    scopus 로고
    • Computational design of a new hydrogen bond network and at least a 300-fold specificity switch at a protein-protein interface
    • Joachimiak LA, Kortemme T, Stoddard BL, Baker D. Computational design of a new hydrogen bond network and at least a 300-fold specificity switch at a protein-protein interface. J Mol Biol 2006; 361: 195-208.
    • (2006) J Mol Biol , vol.361 , pp. 195-208
    • Joachimiak, L.A.1    Kortemme, T.2    Stoddard, B.L.3    Baker, D.4
  • 36
    • 65249171530 scopus 로고    scopus 로고
    • Design of protein interaction specificity gives selective bZIP-binding peptides
    • Grigoryan G, Reinke AW, Keating AE. Design of protein interaction specificity gives selective bZIP-binding peptides. Nature 2009; 458: 859-864.
    • (2009) Nature , vol.458 , pp. 859-864
    • Grigoryan, G.1    Reinke, A.W.2    Keating, A.E.3
  • 37
    • 77954102643 scopus 로고    scopus 로고
    • Protein design in biological networks: from manipulating the input to modifying the output
    • der Sloot AMV, Kiel C, Serrano L, Stricher F. Protein design in biological networks: from manipulating the input to modifying the output. Prot Eng Des Sel 2009; 22: 537-542.
    • (2009) Prot Eng Des Sel , vol.22 , pp. 537-542
    • der Sloot, A.M.V.1    Kiel, C.2    Serrano, L.3    Stricher, F.4
  • 38
    • 77955582352 scopus 로고    scopus 로고
    • Predicting the acid/base behavior of proteins: a constant-pH Monte Carlo approach with generalized Born solvent
    • Aleksandrov A, Polydorides S, Archontis G, Simonson T. Predicting the acid/base behavior of proteins: a constant-pH Monte Carlo approach with generalized Born solvent. J Phys Chem B 2010;114:10634-10648.
    • (2010) J Phys Chem B , vol.114 , pp. 10634-10648
    • Aleksandrov, A.1    Polydorides, S.2    Archontis, G.3    Simonson, T.4
  • 39
    • 0031776357 scopus 로고    scopus 로고
    • Electrostatic contributions to molecular free energies in solution
    • Schaefer M, Vlijmen Hv, Karplus M. Electrostatic contributions to molecular free energies in solution. Adv Prot Chem 1998; 51: 1-57.
    • (1998) Adv Prot Chem , vol.51 , pp. 1-57
    • Schaefer, M.1    Vlijmen, H.2    Karplus, M.3
  • 40
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: insight from computer simulations
    • Warshel A, Parson W. Dynamics of biochemical and biophysical reactions: insight from computer simulations. Q Rev Biophys 2001; 34: 563-679.
    • (2001) Q Rev Biophys , vol.34 , pp. 563-679
    • Warshel, A.1    Parson, W.2
  • 41
    • 0037529067 scopus 로고    scopus 로고
    • Electrostatics and dynamics of proteins
    • Simonson T. Electrostatics and dynamics of proteins. Rep Prog Phys 2003; 66: 737-787.
    • (2003) Rep Prog Phys , vol.66 , pp. 737-787
    • Simonson, T.1
  • 42
    • 33645981305 scopus 로고    scopus 로고
    • Electrostatic calculations: latest methodological advances
    • Koehl P. Electrostatic calculations: latest methodological advances. Curr Opin Struct Biol 2005; 16: 142-151.
    • (2005) Curr Opin Struct Biol , vol.16 , pp. 142-151
    • Koehl, P.1
  • 43
    • 65249154106 scopus 로고    scopus 로고
    • Toward accurate screening in computer-aided enzyme design
    • Roca M, Vardi-Kilshtain A, Warshel A. Toward accurate screening in computer-aided enzyme design. Biochemistry 2009; 48: 3046-3056.
    • (2009) Biochemistry , vol.48 , pp. 3046-3056
    • Roca, M.1    Vardi-Kilshtain, A.2    Warshel, A.3
  • 44
    • 0037229456 scopus 로고    scopus 로고
    • Analyzing six types of protein-protein interfaces
    • Ofran Y, Rost B. Analyzing six types of protein-protein interfaces. JMol Biol 2003; 325: 377-387.
    • (2003) JMol Biol , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 45
    • 32344451863 scopus 로고    scopus 로고
    • Free energy simulations reveal long-range electrostatic interactions and substrate-assisted specificity in an aminoacyl-tRNA synthetase
    • Thompson D, Plateau P, Simonson T. Free energy simulations reveal long-range electrostatic interactions and substrate-assisted specificity in an aminoacyl-tRNA synthetase. ChemBioChem 2006; 7: 337-344.
    • (2006) ChemBioChem , vol.7 , pp. 337-344
    • Thompson, D.1    Plateau, P.2    Simonson, T.3
  • 46
    • 33747671419 scopus 로고    scopus 로고
    • 2+ contributes to amino acid aminoacyl adenylate binding specificity in aspartyl-tRNA synthetase through long range electrostatic interactions
    • 2+ contributes to amino acid aminoacyl adenylate binding specificity in aspartyl-tRNA synthetase through long range electrostatic interactions. J Biol Chem 2006; 281: 23792-23803.
    • (2006) J Biol Chem , vol.281 , pp. 23792-23803
    • Thompson, D.1    Simonson, T.2
  • 47
    • 76649086691 scopus 로고    scopus 로고
    • Alchemical free energy simulations for biological complexes: powerful but temperamental...
    • Aleksandrov A, Thompson D, Simonson T. Alchemical free energy simulations for biological complexes: powerful but temperamental.... J Mol Rec 2010; 23: 117-127.
    • (2010) J Mol Rec , vol.23 , pp. 117-127
    • Aleksandrov, A.1    Thompson, D.2    Simonson, T.3
  • 48
    • 0032488817 scopus 로고    scopus 로고
    • Specific amino acid recognition by Aspartyl-tRNA synthetase studied by free energy simulations
    • Archontis G, Simonson T, Moras D, Karplus M. Specific amino acid recognition by Aspartyl-tRNA synthetase studied by free energy simulations. J Mol Biol 1998; 275: 823-846.
    • (1998) J Mol Biol , vol.275 , pp. 823-846
    • Archontis, G.1    Simonson, T.2    Moras, D.3    Karplus, M.4
  • 49
    • 0035895423 scopus 로고    scopus 로고
    • Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations
    • Archontis G, Simonson T, Karplus M. Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. J Mol Biol 2001; 306: 307-327.
    • (2001) J Mol Biol , vol.306 , pp. 307-327
    • Archontis, G.1    Simonson, T.2    Karplus, M.3
  • 50
    • 0036286654 scopus 로고    scopus 로고
    • Free-energy Simulations come of age: protein-ligand recognition
    • Simonson T, Archontis G, Karplus M. Free-energy Simulations come of age: protein-ligand recognition. Acc Chem Res 2002; 35: 430-437.
    • (2002) Acc Chem Res , vol.35 , pp. 430-437
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 51
    • 13944256616 scopus 로고    scopus 로고
    • 'solvated rotamer' approach to modeling water-mediated hydrogen bonds at protein-protein interfaces
    • Jiang L, Kuhlman B, Kortemme TA, Baker DA. 'solvated rotamer' approach to modeling water-mediated hydrogen bonds at protein-protein interfaces. Proteins 2005; 58: 893-904.
    • (2005) Proteins , vol.58 , pp. 893-904
    • Jiang, L.1    Kuhlman, B.2    Kortemme, T.A.3    Baker, D.A.4
  • 52
    • 0032968133 scopus 로고    scopus 로고
    • Implicit solvent models
    • Roux B, Simonson T. Implicit solvent models. Biophys Chem 1999; 78: 1-20.
    • (1999) Biophys Chem , vol.78 , pp. 1-20
    • Roux, B.1    Simonson, T.2
  • 53
    • 0035312551 scopus 로고    scopus 로고
    • Macromolecular electrostatics: continuum models and their growing pains
    • Simonson T. Macromolecular electrostatics: continuum models and their growing pains. Curr Opin Struct Biol 2001; 11: 243-252.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 243-252
    • Simonson, T.1
  • 54
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D, McClachlan A. Solvation energy in protein folding and binding. Nature 1986; 319: 199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McClachlan, A.2
  • 55
    • 0023338543 scopus 로고
    • Accessible surface areas as a measure of the thermodynamic hydration parameters of peptides
    • Ooi T, Oobatake M, Nemethy G, Scheraga H. Accessible surface areas as a measure of the thermodynamic hydration parameters of peptides. Proc Natl Acad Sci USA 1987; 84: 3086-3090.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3086-3090
    • Ooi, T.1    Oobatake, M.2    Nemethy, G.3    Scheraga, H.4
  • 56
    • 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. Protein Sci 1992; 1: 227-235.
    • (1992) Protein Sci , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 57
    • 34248586877 scopus 로고    scopus 로고
    • Computational sidechain placement and protein mutagenesis with implicit solvent models
    • Lopes A, Alexandrov A, Bathelt C, Archontis G, Simonson T. Computational sidechain placement and protein mutagenesis with implicit solvent models. Proteins 2007; 67: 853-867.
    • (2007) Proteins , vol.67 , pp. 853-867
    • Lopes, A.1    Alexandrov, A.2    Bathelt, C.3    Archontis, G.4    Simonson, T.5
  • 58
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat B, Mayo S. Protein design automation. Protein Sci 1996; 5: 895-903.
    • (1996) Protein Sci , vol.5 , pp. 895-903
    • Dahiyat, B.1    Mayo, S.2
  • 59
    • 0036138028 scopus 로고    scopus 로고
    • Evaluation of a fast implicit solvent model for molecular dynamics simulations
    • Ferrara P, Apostolakis J, Caflisch A. Evaluation of a fast implicit solvent model for molecular dynamics simulations. Proteins 2002; 46: 24-33.
    • (2002) Proteins , vol.46 , pp. 24-33
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 60
    • 0037428393 scopus 로고    scopus 로고
    • Automatic sequence design of MHC class-I binding peptides impairing CD8+ T-cell recognition
    • Ogata K, Jaramillo A, Cohen W, Briand J, Conana F, Wodak S. Automatic sequence design of MHC class-I binding peptides impairing CD8+ T-cell recognition. J Biol Chem 2003; 278: 1281-1290.
    • (2003) J Biol Chem , vol.278 , pp. 1281-1290
    • Ogata, K.1    Jaramillo, A.2    Cohen, W.3    Briand, J.4    Conana, F.5    Wodak, S.6
  • 61
    • 4243463817 scopus 로고
    • Electrostatics in biomolecular structure and dynamics
    • Davis ME, McCammon JA. Electrostatics in biomolecular structure and dynamics. Chem Rev 1990; 90: 509-521.
    • (1990) Chem Rev , vol.90 , pp. 509-521
    • Davis, M.E.1    McCammon, J.A.2
  • 62
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B, Nicholls A. Classical electrostatics in biology and chemistry. Science 1995; 268: 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 63
    • 0043245780 scopus 로고    scopus 로고
    • Insight into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke H, Kiel C, Case D. Insight into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J Mol Biol 2003; 330: 891-913.
    • (2003) J Mol Biol , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.3
  • 64
    • 0042139644 scopus 로고    scopus 로고
    • Comparison of generalized Born and Poisson models: energetics and dynamics of HIV protease
    • David L, Luo R, Gilson M. Comparison of generalized Born and Poisson models: energetics and dynamics of HIV protease. J Comp Chem 2000; 21: 295-309.
    • (2000) J Comp Chem , vol.21 , pp. 295-309
    • David, L.1    Luo, R.2    Gilson, M.3
  • 65
    • 1842454839 scopus 로고    scopus 로고
    • Energy functions for protein design I: efficient and accurate continuum electrostatics and solvation
    • Pokala N, Handel TM. Energy functions for protein design I: efficient and accurate continuum electrostatics and solvation. Protien Sci 2004; 13: 925-936.
    • (2004) Protien Sci , vol.13 , pp. 925-936
    • Pokala, N.1    Handel, T.M.2
  • 66
    • 0033550206 scopus 로고    scopus 로고
    • De novo protein design. I. In search of stability and specificity
    • Koehl P, Levitt M. De novo protein design. I. In search of stability and specificity. J Mol Biol 1999; 293: 1161-.
    • (1999) J Mol Biol , vol.293 , pp. 1161
    • Koehl, P.1    Levitt, M.2
  • 67
    • 0034682869 scopus 로고    scopus 로고
    • Automatic protein design with all-atom force-fields by exact and heuristic optimization
    • Wernisch L, Henry S, Wodak S. Automatic protein design with all-atom force-fields by exact and heuristic optimization. J Mol Biol 2001; 301: 713-736.
    • (2001) J Mol Biol , vol.301 , pp. 713-736
    • Wernisch, L.1    Henry, S.2    Wodak, S.3
  • 68
    • 17744382377 scopus 로고    scopus 로고
    • One- and two-body decomposable Poisson-Boltzmann methods for protein design calculations
    • Marshall SA, Vizcarra CL, Mayo SL. One- and two-body decomposable Poisson-Boltzmann methods for protein design calculations. Protein Sci 2005; 14: 1293-1304.
    • (2005) Protein Sci , vol.14 , pp. 1293-1304
    • Marshall, S.A.1    Vizcarra, C.L.2    Mayo, S.L.3
  • 69
    • 27744498365 scopus 로고    scopus 로고
    • Electrostatics in computational protein design
    • Vizcarra CL, Mayo SL. Electrostatics in computational protein design. Curr Opin Chem Biol 2005; 9: 622-626.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 622-626
    • Vizcarra, C.L.1    Mayo, S.L.2
  • 70
    • 42149085208 scopus 로고    scopus 로고
    • An improved pairwise decomposable finite-difference Poisson-Boltzmann method for computational protein design
    • Vizcarra CL, Zhang N, Marshall SA, Wingreen NS, Zeng C, Mayo SL. An improved pairwise decomposable finite-difference Poisson-Boltzmann method for computational protein design. J Comp Chem 2008; 29: 1153-1162.
    • (2008) J Comp Chem , vol.29 , pp. 1153-1162
    • Vizcarra, C.L.1    Zhang, N.2    Marshall, S.A.3    Wingreen, N.S.4    Zeng, C.5    Mayo, S.L.6
  • 71
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still WC, Tempczyk A, Hawley R, 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.3    Hendrickson, T.4
  • 72
    • 0033654297 scopus 로고    scopus 로고
    • Generalized Born models of macromolecular solvation effects
    • Bashford D, Case D. Generalized Born models of macromolecular solvation effects. Ann Rev Phys Chem 2000; 51: 129-152.
    • (2000) Ann Rev Phys Chem , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.2
  • 73
    • 1942456697 scopus 로고    scopus 로고
    • Recent advances in the development and application of implicit solvent models in biomolecular simulations
    • Feig M, Brooks CL, III. Recent advances in the development and application of implicit solvent models in biomolecular simulations. Curr Opin Struct Biol 2004; 14: 217-224.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 217-224
    • Feig, M.1    Brooks III, C.L.2
  • 74
    • 41949100049 scopus 로고    scopus 로고
    • Recent advances in implicit-solvent based methods for biomolecular simulations
    • Chen J, Brooks CL, III, Khandogin J. Recent advances in implicit-solvent based methods for biomolecular simulations. Curr Opin Struct Biol 2008; 18: 140-148.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 140-148
    • Chen, J.1    Brooks III, C.L.2    Khandogin, J.3
  • 75
    • 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
  • 76
    • 4043171970 scopus 로고    scopus 로고
    • A fast analytical method for hte calculation of approximate Born radii
    • Qiu D, Shenkin P, Hollinger F, Still W. A fast analytical method for hte 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.2    Hollinger, F.3    Still, W.4
  • 77
    • 0001246294 scopus 로고    scopus 로고
    • Generalized Born model based on a surface-area formulation
    • Gosh A, Rapp C, Friesner RA. Generalized Born model based on a surface-area formulation. J Phys Chem B 1998; 102: 10983-10990.
    • (1998) J Phys Chem B , vol.102 , pp. 10983-10990
    • Gosh, A.1    Rapp, C.2    Friesner, R.A.3
  • 78
    • 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 Comp Chem 1999; 20: 322-335.
    • (1999) J Comp Chem , vol.20 , pp. 322-335
    • Wagner, F.1    Simonson, T.2
  • 79
    • 71649114292 scopus 로고    scopus 로고
    • Amyloid-like self-assembly of peptide sequences from the adenovirus fiber shaft: insights from molecular dynamics simulations
    • Tamamis P, Kasotakis E, Mitraki A, Archontis G. Amyloid-like self-assembly of peptide sequences from the adenovirus fiber shaft: insights from molecular dynamics simulations. J Phys Chem B 2009; 113: 15639-15647.
    • (2009) J Phys Chem B , vol.113 , pp. 15639-15647
    • Tamamis, P.1    Kasotakis, E.2    Mitraki, A.3    Archontis, G.4
  • 81
    • 20644449471 scopus 로고    scopus 로고
    • Modification of the generalized Born model suitable for macromolecules
    • Onufriev A, Bashford D, Case D. Modification of the generalized Born model suitable for macromolecules. J Phys Chem B 2000; 104: 3712-3720.
    • (2000) J Phys Chem B , vol.104 , pp. 3712-3720
    • Onufriev, A.1    Bashford, D.2    Case, D.3
  • 82
    • 4043132337 scopus 로고    scopus 로고
    • Constant pH molecular dynamics using continuous titration coordinates
    • Lee M, Salsbury F, Brooks CL, III. Constant pH molecular dynamics using continuous titration coordinates. Proteins 2004; 56: 738-752.
    • (2004) Proteins , vol.56 , pp. 738-752
    • Lee, M.1    Salsbury, F.2    Brooks III, C.L.3
  • 83
    • 9244223045 scopus 로고    scopus 로고
    • Constant pH molecular dynamics in generalized Born implicit solvent
    • Mongan J, Case DA, McCammon JA. Constant pH molecular dynamics in generalized Born implicit solvent. J Comp Chem 2004; 25: 2038-2048.
    • (2004) J Comp Chem , vol.25 , pp. 2038-2048
    • Mongan, J.1    Case, D.A.2    McCammon, J.A.3
  • 84
    • 33747131772 scopus 로고    scopus 로고
    • Toward the accurate first-principles prediction of ionization equilibria in proteins
    • Khandogin J, Brooks CL, III. Toward the accurate first-principles prediction of ionization equilibria in proteins. Biochemistry 2006; 45: 9363-9373.
    • (2006) Biochemistry , vol.45 , pp. 9363-9373
    • Khandogin, J.1    Brooks III, C.L.2
  • 85
    • 0035501755 scopus 로고    scopus 로고
    • Protein molecular dynamics with the Generalized Born/ACE solvent model
    • Calimet N, Schaefer M, Simonson T. Protein molecular dynamics with the Generalized Born/ACE solvent model. Proteins 2001; 45: 144-158.
    • (2001) Proteins , vol.45 , pp. 144-158
    • Calimet, N.1    Schaefer, M.2    Simonson, T.3
  • 86
    • 0037174385 scopus 로고    scopus 로고
    • All-atom structure prediction and folding simulations of a stable protein
    • Simmerling C, Strockbine B, Roitberg A. All-atom structure prediction and folding simulations of a stable protein. J Am Chem Soc 2002; 124: 11258-11259.
    • (2002) J Am Chem Soc , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.3
  • 87
    • 0033214412 scopus 로고    scopus 로고
    • Exhaustive docking of molecular fragments with electrostatic solvation
    • Majeux N, Scarsi M, Apostolakis J, Ehrhardt C, Caflisch A. Exhaustive docking of molecular fragments with electrostatic solvation. Proteins 1999; 38: 88-105.
    • (1999) Proteins , vol.38 , pp. 88-105
    • Majeux, N.1    Scarsi, M.2    Apostolakis, J.3    Ehrhardt, C.4    Caflisch, A.5
  • 88
    • 33744821352 scopus 로고    scopus 로고
    • Electrostatics of ligand binding: parameterization of the generalized Born model and comparison with the Poisson-Boltzmann approach
    • Liu HY, Zou X. Electrostatics of ligand binding: parameterization of the generalized Born model and comparison with the Poisson-Boltzmann approach. J Phys Chem B 2006; 110: 9304-9313.
    • (2006) J Phys Chem B , vol.110 , pp. 9304-9313
    • Liu, H.Y.1    Zou, X.2
  • 89
    • 0037174385 scopus 로고    scopus 로고
    • All-atom structure prediction and folding simulations of a stable protein
    • Simmerling C, Strockbine B, Roitberg A. All-atom structure prediction and folding simulations of a stable protein. J Am Chem Soc 2002; 124: 11258-11259.
    • (2002) J Am Chem Soc , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.3
  • 90
    • 33645408056 scopus 로고    scopus 로고
    • Balancing solvation and intramolecular interactions: towards a consistent generalized Born force field
    • Chen J, Im W, Brooks CL, III. Balancing solvation and intramolecular interactions: towards a consistent generalized Born force field. J Am Chem Soc 2006; 128: 3728-3736.
    • (2006) J Am Chem Soc , vol.128 , pp. 3728-3736
    • Chen, J.1    Im, W.2    Brooks III, C.L.3
  • 91
    • 33845633270 scopus 로고    scopus 로고
    • Direct folding simulation of alpha-helices and beta-hairpins based on a single all-atom force field with an implicit solvation model
    • Jang S, Kim E, Pak Y. Direct folding simulation of alpha-helices and beta-hairpins based on a single all-atom force field with an implicit solvation model. Proteins 2007; 66: 53-60.
    • (2007) Proteins , vol.66 , pp. 53-60
    • Jang, S.1    Kim, E.2    Pak, Y.3
  • 92
    • 34247639441 scopus 로고    scopus 로고
    • Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulations
    • Lei H, Wu C, Liu H, Duan Y. Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulations. Proc Natl Acad Sci USA 2007; 104: 4925-4930.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4925-4930
    • Lei, H.1    Wu, C.2    Liu, H.3    Duan, Y.4
  • 93
    • 0347062349 scopus 로고    scopus 로고
    • Xray structure refinement of proteins with the generalized Born solvent model
    • Moulinier L, Case DA, Simonson T. Xray structure refinement of proteins with the generalized Born solvent model. Acta Cryst D 2003; 59: 2094-2103.
    • (2003) Acta Cryst D , vol.59 , pp. 2094-2103
    • Moulinier, L.1    Case, D.A.2    Simonson, T.3
  • 94
    • 10344226224 scopus 로고    scopus 로고
    • Refinement of NMR structures using implicit solvent and advanced sampling techniques
    • Chen J, Im W, Brooks CL, III. Refinement of NMR structures using implicit solvent and advanced sampling techniques. J Am Chem Soc 2004; 126: 16038-16047.
    • (2004) J Am Chem Soc , vol.126 , pp. 16038-16047
    • Chen, J.1    Im, W.2    Brooks III, C.L.3
  • 95
    • 35048835681 scopus 로고    scopus 로고
    • Assessment of detection and refinement strategies for de novo protein structures using force field and statistical potentials
    • Lee MS, Olson MA. Assessment of detection and refinement strategies for de novo protein structures using force field and statistical potentials. J Chem Theory Comput 2007; 3: 312-324.
    • (2007) J Chem Theory Comput , vol.3 , pp. 312-324
    • Lee, M.S.1    Olson, M.A.2
  • 96
    • 44949229094 scopus 로고    scopus 로고
    • Design of protein-ligand binding based on the molecular-mechanics energy model
    • Boas FE, Harbury PB. Design of protein-ligand binding based on the molecular-mechanics energy model. J Mol Biol 2008; 380: 415-424.
    • (2008) J Mol Biol , vol.380 , pp. 415-424
    • Boas, F.E.1    Harbury, P.B.2
  • 98
    • 42149177372 scopus 로고    scopus 로고
    • Computational protein design: software implementation, parameter optimization and performance of a simple model
    • am Buch MS, Lopes A, Mignon D, Simonson T. Computational protein design: software implementation, parameter optimization and performance of a simple model. J Comp Chem 2008; 29: 1092-1102.
    • (2008) J Comp Chem , vol.29 , pp. 1092-1102
    • am Buch, M.S.1    Lopes, A.2    Mignon, D.3    Simonson, T.4
  • 99
    • 42149195952 scopus 로고    scopus 로고
    • Testing the Coulomb/Accessible Surface Area solvent model for protein stability, ligand binding and protein design
    • am Buch MS, Lopes A, Amara N, Bathelt C, Simonson T. Testing the Coulomb/Accessible Surface Area solvent model for protein stability, ligand binding and protein design. BMC Bioinformatics 2008; 9: 148-163.
    • (2008) BMC Bioinformatics , vol.9 , pp. 148-163
    • am Buch, M.S.1    Lopes, A.2    Amara, N.3    Bathelt, C.4    Simonson, T.5
  • 100
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack S. Eleven down and nine to go. Nat Struct Biol 1995; 2: 824-831.
    • (1995) Nat Struct Biol , vol.2 , pp. 824-831
    • Cusack, S.1
  • 101
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional consideration of the aminoacylation reaction
    • Arnez J, Moras D. Structural and functional consideration of the aminoacylation reaction. Trends Biochem Sci 1997; 22: 211-216.
    • (1997) Trends Biochem Sci , vol.22 , pp. 211-216
    • Arnez, J.1    Moras, D.2
  • 103
    • 0027497871 scopus 로고
    • Modification of the amino acid specificity of tyr-tRNA synthetase by protein engineering
    • de Prat Gay G, Duckworth H, Fersht A. Modification of the amino acid specificity of tyr-tRNA synthetase by protein engineering. FEBS Lett 1993; 318: 167-171.
    • (1993) FEBS Lett , vol.318 , pp. 167-171
    • de Prat Gay, G.1    Duckworth, H.2    Fersht, A.3
  • 104
    • 0032508381 scopus 로고    scopus 로고
    • Switching the amino acid specificity of an aminoacyl-tRNA synthetase
    • Agou F, Quevillon S, Kerjan P, Mirande M. Switching the amino acid specificity of an aminoacyl-tRNA synthetase. Biochemistry 1998; 37: 11309-11314.
    • (1998) Biochemistry , vol.37 , pp. 11309-11314
    • Agou, F.1    Quevillon, S.2    Kerjan, P.3    Mirande, M.4
  • 106
    • 27744485401 scopus 로고    scopus 로고
    • Adding amino acids to the genetic repertoire
    • Xie J, Schultz P. Adding amino acids to the genetic repertoire. Curr Opin Chem Biol 2005; 9: 548-554.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 548-554
    • Xie, J.1    Schultz, P.2
  • 107
    • 42449089814 scopus 로고    scopus 로고
    • Probing electrostatic interactions and ligand binding in aspartyl-tRNA synthetase through site-directed mutagenesis and computer simulations
    • Thompson D, Lazennec C, Plateau P, Simonson T. Probing electrostatic interactions and ligand binding in aspartyl-tRNA synthetase through site-directed mutagenesis and computer simulations. Proteins 2008; 71: 1450-1460.
    • (2008) Proteins , vol.71 , pp. 1450-1460
    • Thompson, D.1    Lazennec, C.2    Plateau, P.3    Simonson, T.4
  • 108
    • 0032525301 scopus 로고    scopus 로고
    • The crystal structure of asparaginyl-tRNA synthetase from thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid
    • Berthet-Colominas C, Seignovert L, Hartlein M, Grotli M, Cusack S. The crystal structure of asparaginyl-tRNA synthetase from thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid. EMBO J 1998; 17: 2947-2960.
    • (1998) EMBO J , vol.17 , pp. 2947-2960
    • Berthet-Colominas, C.1    Seignovert, L.2    Hartlein, M.3    Grotli, M.4    Cusack, S.5
  • 110
    • 0002636134 scopus 로고
    • Pairwise descreening of solute charges from a dielectric medium
    • Hawkins G, Cramer C, Truhlar D. Pairwise 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.1    Cramer, C.2    Truhlar, D.3
  • 111
    • 29144468591 scopus 로고    scopus 로고
    • A residue-pairwise Generalized Born scheme suitable for protein design calculations
    • Archontis G, Simonson T. A residue-pairwise Generalized Born scheme suitable for protein design calculations. J Phys Chem B 2005; 109: 22667-22673.
    • (2005) J Phys Chem B , vol.109 , pp. 22667-22673
    • Archontis, G.1    Simonson, T.2
  • 112
    • 0033571581 scopus 로고    scopus 로고
    • Synthesis of aspartyl-tRNA(asp) in Escherichia coli: a snapshot of the second step
    • Eiler S, Dock-Bregeon A, Moulinier L, Thierry J, Moras D. Synthesis of aspartyl-tRNA(asp) in Escherichia coli: a snapshot of the second step. EMBO J 1999; 18: 6532-6541.
    • (1999) EMBO J , vol.18 , pp. 6532-6541
    • Eiler, S.1    Dock-Bregeon, A.2    Moulinier, L.3    Thierry, J.4    Moras, D.5
  • 113
    • 0026179489 scopus 로고
    • A new approach to the rapid determination of protein side chain conformations
    • Tuffery P, Etchebest C, Hazout S, Lavery R. A new approach to the rapid determination of protein side chain conformations. J Biomol Struct Dyn 1991; 8: 1267.
    • (1991) J Biomol Struct Dyn , vol.8 , pp. 1267
    • Tuffery, P.1    Etchebest, C.2    Hazout, S.3    Lavery, R.4
  • 116
    • 0022531877 scopus 로고
    • Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetase
    • Ho CK, Fersht AR. Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetase. Biochemistry 1986; 25: 1891-1897.
    • (1986) Biochemistry , vol.25 , pp. 1891-1897
    • Ho, C.K.1    Fersht, A.R.2
  • 117
    • 0022471120 scopus 로고
    • Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase
    • Wells TN, Fersht AR. Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase. Biochemistry 1986; 25: 1881-1886.
    • (1986) Biochemistry , vol.25 , pp. 1881-1886
    • Wells, T.N.1    Fersht, A.R.2
  • 118
    • 0023662562 scopus 로고
    • Structure-reactivity relationships in engineered proteins:analysis of use of binding energy by linear free energy relationships
    • Fersht AR, Leatherbarrow RJ, Wells TN. Structure-reactivity relationships in engineered proteins:analysis of use of binding energy by linear free energy relationships. Biochemistry 1987; 26: 6030-6038.
    • (1987) Biochemistry , vol.26 , pp. 6030-6038
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.3
  • 119
    • 0027497871 scopus 로고
    • Modification of the amino acid specificity of tyrosyl-tRNA synthetase by protein engineering
    • de Prat Gay G, Duckworth HW, Fersht AR. Modification of the amino acid specificity of tyrosyl-tRNA synthetase by protein engineering. FEBS Letters 1993; 318: 167-171.
    • (1993) FEBS Letters , vol.318 , pp. 167-171
    • de Prat Gay, G.1    Duckworth, H.W.2    Fersht, A.R.3
  • 120
    • 0027751260 scopus 로고
    • Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase
    • First EA, Fersht AR. Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase. Biochemistry 1993; 32: 13658-13663.
    • (1993) Biochemistry , vol.32 , pp. 13658-13663
    • First, E.A.1    Fersht, A.R.2
  • 122
    • 0032528684 scopus 로고    scopus 로고
    • 2+ site to replace a structurally conserved arginine in the catalytic center of histidyl-tRNA synthetase by computer experiments
    • 2+ site to replace a structurally conserved arginine in the catalytic center of histidyl-tRNA synthetase by computer experiments. Proteins 1998; 32: 362-380.
    • (1998) Proteins , vol.32 , pp. 362-380
    • Arnez, J.1    Flanagan, K.2    Moras, D.3    Simonson, T.4
  • 124
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: an N log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle Mesh Ewald: an N log(N) method for Ewald sums in large systems. J Chem Phys 1993; 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 125
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics method
    • Nose S. A unified formulation of the constant temperature molecular dynamics method. J Chem Phys 1984; 81: 511-519.
    • (1984) J Chem Phys , vol.81 , pp. 511-519
    • Nose, S.1
  • 126
    • 0001538909 scopus 로고
    • Canonical dynamics: equilibrium phase-space distributions
    • Hoover W. Canonical dynamics: equilibrium phase-space distributions. Phys Rev A 1985; 31: 1695-1697.
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.1
  • 127
    • 36449007836 scopus 로고
    • Constant-pressure molecular-dynamics simulation: the Langevin piston method
    • Feller S, Zhang Y, Pastor RW, Brooks B. Constant-pressure molecular-dynamics simulation: the Langevin piston method. J Chem Phys 1995; 103: 4613-4621.
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.4
  • 128
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977; 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 130
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: a computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • Im W, Beglov D, Roux B. Continuum solvation model: a computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation. Comp Phys Comm 1998; 111: 59-75.
    • (1998) Comp Phys Comm , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 132
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in proteins and peptides
    • Myers JK, Pace CN, Scholtz JM. Helix propensities are identical in proteins and peptides. Biochemistry 1997; 36: 10923-10929.
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 133
    • 0030925636 scopus 로고    scopus 로고
    • The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model
    • Yang J, Spek EJ, Gong Y, Zhou H, Kallenbach NR. The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model. Protein Sci 1997; 6: 1-9.
    • (1997) Protein Sci , vol.6 , pp. 1-9
    • Yang, J.1    Spek, E.J.2    Gong, Y.3    Zhou, H.4    Kallenbach, N.R.5
  • 134
    • 0027249564 scopus 로고
    • Residue helix parameters obtained from dichroic analysis of peptides of defined sequence
    • Park SH, Shalongo W, Stellwagen E. Residue helix parameters obtained from dichroic analysis of peptides of defined sequence. Biochemistry 1993; 32: 7048-7053.
    • (1993) Biochemistry , vol.32 , pp. 7048-7053
    • Park, S.H.1    Shalongo, W.2    Stellwagen, E.3
  • 135
  • 136
    • 33847768547 scopus 로고    scopus 로고
    • '-Pyrophosphate-linked dinucleotide inhibitors: a molecular dynamics/continuum electrostatics analysis
    • '-Pyrophosphate-linked dinucleotide inhibitors: a molecular dynamics/continuum electrostatics analysis. Biophys J 2007; 92: 1659-1672.
    • (2007) Biophys J , vol.92 , pp. 1659-1672
    • Polydoridis, S.1    Leonidas, D.D.2    Oikonomakos, N.G.3    Archontis, G.4
  • 137
    • 1342310514 scopus 로고    scopus 로고
    • Improved side-chain prediction accuracy using an ab initio potential energy function and a very large rotamer library
    • Peterson RW, Dutton PL, Wand AJ. Improved side-chain prediction accuracy using an ab initio potential energy function and a very large rotamer library. Protein Sci 2004; 13: 735-751.
    • (2004) Protein Sci , vol.13 , pp. 735-751
    • Peterson, R.W.1    Dutton, P.L.2    Wand, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.