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Volumn 23, Issue 2, 2010, Pages 142-152

MM-GBSA binding free energy decomposition and T cell receptor engineering

Author keywords

Free energy simulations; Protein engineering; T cell receptor

Indexed keywords


EID: 76649121529     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.1005     Document Type: Article
Times cited : (79)

References (71)
  • 1
    • 0348189638 scopus 로고
    • Solubility of nonelectrolytes in polar solvents. V. Estimation of the solubility of aliphatic monofunctional compounds in water using a molecular surface area approach
    • Amidon GL, Yalkowsky SH, Anik ST, Valvani SC. 1975. Solubility of nonelectrolytes in polar solvents. V. Estimation of the solubility of aliphatic monofunctional compounds in water using a molecular surface area approach. J. Phys. Chem. 79: 2239-2246.
    • (1975) J. Phys. Chem. , vol.79 , pp. 2239-2246
    • Amidon, G.L.1    Yalkowsky, S.H.2    Anik, S.T.3    Valvani, S.C.4
  • 2
    • 69749120935 scopus 로고    scopus 로고
    • Quantitative prediction of fold resistance for inhibitors of EGFR
    • Balius TE, Rizzo RC. 2009. Quantitative prediction of fold resistance for inhibitors of EGFR. Biochemistry 48: 8435-8448.
    • (2009) Biochemistry , vol.48 , pp. 8435-8448
    • Balius, T.E.1    Rizzo, R.C.2
  • 3
    • 0023106632 scopus 로고
    • Calculation of the relative change in binding free energy of a protein-inhibitor complex
    • Bash PA, Singh UC, Brown FK, Langridge R, Kollman PA. 1987. Calculation of the relative change in binding free energy of a protein-inhibitor complex. Science 235: 574-576.
    • (1987) Science , vol.235 , pp. 574-576
    • Bash, P.A.1    Singh, U.C.2    Brown, F.K.3    Langridge, R.4    Kollman, P.A.5
  • 5
    • 25444447108 scopus 로고    scopus 로고
    • Scoring binding affinity of multiple ligands using implicit solvent and a single molecular dynamics trajectory: Application to influenza neuraminidase
    • Bonnet P, Bryce RA. 2005. Scoring binding affinity of multiple ligands using implicit solvent and a single molecular dynamics trajectory: application to influenza neuraminidase. J. Mol. Graph Model 24: 147-156.
    • (2005) J. Mol. Graph Model , vol.24 , pp. 147-156
    • Bonnet, P.1    Bryce, R.A.2
  • 9
    • 12344322695 scopus 로고    scopus 로고
    • Highaffinity, peptide-specific T cell receptors can be generated by mutations in CDR1, CDR2 or CDR3
    • Chlewicki LK, Holler PD, Monti BC, Clutter MR, Kranz DM. 2005. Highaffinity, peptide-specific T cell receptors can be generated by mutations in CDR1, CDR2 or CDR3. J. Mol. Biol. 346: 223-239.
    • (2005) J. Mol. Biol. , vol.346 , pp. 223-239
    • Chlewicki, L.K.1    Holler, P.D.2    Monti, B.C.3    Clutter, M.R.4    Kranz, D.M.5
  • 11
    • 33645677701 scopus 로고    scopus 로고
    • Modeling the peptide-T cell receptor interaction by the comparative molecular similarity indices analysissoft independent modeling of class analogy technique
    • Doytchinova IA, Flower DR. 2006. Modeling the peptide-T cell receptor interaction by the comparative molecular similarity indices analysissoft independent modeling of class analogy technique. J. Med. Chem. 49: 2193-2199.
    • (2006) J. Med. Chem. , vol.49 , pp. 2193-2199
    • Doytchinova, I.A.1    Flower, D.R.2
  • 12
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack RL, Jr. 2002. Rotamer libraries in the 21st century. Curr. Opin. Struct. Biol. 12: 431-440.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack Jr., R.L.1
  • 13
    • 33645498495 scopus 로고    scopus 로고
    • Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity
    • Dunn SM, Rizkallah PJ, Baston E, Mahon T, Cameron B, Moysey R, Gao F, Sami M, Boulter J, Li Y, Jakobsen BK. 2006. Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity. Protein Sci. 15: 710-721.
    • (2006) Protein Sci. , vol.15 , pp. 710-721
    • Dunn, S.M.1    Rizkallah, P.J.2    Baston, E.3    Mahon, T.4    Cameron, B.5    Moysey, R.6    Gao, F.7    Sami, M.8    Boulter, J.9    Li, Y.10    Jakobsen, B.K.11
  • 14
    • 51949096545 scopus 로고    scopus 로고
    • Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin
    • Espinoza-Fonseca LM, Kast D, Thomas DD. 2008. Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin. J. Am. Chem. Soc. 130: 12208-12209.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12208-12209
    • Espinoza-Fonseca, L.M.1    Kast, D.2    Thomas, D.D.3
  • 16
    • 15244349255 scopus 로고    scopus 로고
    • Application of MM/PBSAcolony free energy to loop decoy discrimination: Toward correlation between energy and root mean square deviation
    • Fogolari F, Tosatto SC. 2005. Application of MM/PBSAcolony free energy to loop decoy discrimination: toward correlation between energy and root mean square deviation. Protein Sci. 14: 889-901.
    • (2005) Protein Sci. , vol.14 , pp. 889-901
    • Fogolari, F.1    Tosatto, S.C.2
  • 17
    • 33845335781 scopus 로고    scopus 로고
    • Towards predictive ligand design with freeenergy based computational methods?
    • Foloppe N, Hubbard R. 2006. Towards predictive ligand design with freeenergy based computational methods? Curr. Med. Chem. 13: 3583-3608.
    • (2006) Curr. Med. Chem , vol.13 , pp. 3583-3608
    • Foloppe, N.1    Hubbard, R.2
  • 19
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson MK, Honig B. 1988a. Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis. Proteins 4: 7-18.
    • (1988) Proteins , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.2
  • 20
    • 0023899747 scopus 로고
    • Energetics of charge-charge interactions in proteins
    • Gilson MK, Honig BH. 1988b. Energetics of charge-charge interactions in proteins. Proteins 3: 32-52.
    • (1988) Proteins , vol.3 , pp. 32-52
    • Gilson, M.K.1    Honig, B.H.2
  • 21
    • 0043245780 scopus 로고    scopus 로고
    • Insights 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 DA. 2003. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J. Mol. Biol. 330: 891-913.
    • (2003) J. Mol. Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 22
    • 3042806330 scopus 로고    scopus 로고
    • Change in protein flexibility upon complex formation: Analysis of Ras-Raf using molecular dynamics and a molecular framework approach
    • Gohlke H, Kuhn LA, Case DA. 2004. Change in protein flexibility upon complex formation: analysis of Ras-Raf using molecular dynamics and a molecular framework approach. Proteins 56: 322-337.
    • (2004) Proteins , vol.56 , pp. 322-337
    • Gohlke, H.1    Kuhn, L.A.2    Case, D.A.3
  • 23
    • 0037234043 scopus 로고    scopus 로고
    • Free energy calculations for theophylline binding to an RNA aptamer: MM-PBSA and comparison of thermodynamic integration methods
    • Gouda H, Kuntz ID, Case DA, Kollman PA. 2003. Free energy calculations for theophylline binding to an RNA aptamer: MM-PBSA and comparison of thermodynamic integration methods. Biopolymers 68: 16-34.
    • (2003) Biopolymers , vol.68 , pp. 16-34
    • Gouda, H.1    Kuntz, I.D.2    Case, D.A.3    Kollman, P.A.4
  • 24
    • 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 W, Li M, Weng Z. 2009. Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC. Proteins 74: 948-960.
    • (2009) Proteins , vol.74 , pp. 948-960
    • Haidar, J.N.1    Pierce, B.2    Yu, Y.3    Tong, W.4    Li, M.5    Weng, Z.6
  • 26
    • 33947644064 scopus 로고    scopus 로고
    • Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: Mechanism for binding and drug resistance
    • Hou T, Yu R. 2007. Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance. J. Med. Chem. 50: 1177-1188.
    • (2007) J. Med. Chem. , vol.50 , pp. 1177-1188
    • Hou, T.1    Yu, R.2
  • 27
    • 0032528403 scopus 로고    scopus 로고
    • The efficiency of antigen recognition by CD8{thorn}CTL clones is determined by the frequency of serial TCR engagement
    • Hudrisier D, Kessler B, Valitutti S, Horvath C, Cerottini JC, Luescher IF. 1998. The efficiency of antigen recognition by CD8{thorn}CTL clones is determined by the frequency of serial TCR engagement. J. Immunol. 161: 553-562.
    • (1998) J. Immunol. , vol.161 , pp. 553-562
    • Hudrisier, D.1    Kessler, B.2    Valitutti, S.3    Horvath, C.4    Cerottini, J.C.5    Luescher, I.F.6
  • 28
    • 0037079570 scopus 로고    scopus 로고
    • Computational alanine scanning of the 1: 1 human growth hormone-receptor complex
    • Huo S, Massova I, Kollman PA. 2002. Computational alanine scanning of the 1: 1 human growth hormone-receptor complex. J. Comp. Chem. 23: 15-27.
    • (2002) J. Comp. Chem , vol.23 , pp. 15-27
    • Huo, S.1    Massova, I.2    Kollman, P.A.3
  • 30
    • 69249158062 scopus 로고    scopus 로고
    • Computational design of affinity and specificity at protein-protein interfaces
    • Karanicolas J, Kuhlman B. 2009. Computational design of affinity and specificity at protein-protein interfaces. Curr. Opin. Struct. Biol. 19: 458-463.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 458-463
    • Karanicolas, J.1    Kuhlman, B.2
  • 31
    • 33646471468 scopus 로고
    • Statistical mechanics of fluid mixture
    • Kirkwood JG. 1935. Statistical mechanics of fluid mixture. J. Chem. Phys. 3: 300-313.
    • (1935) J. Chem. Phys. , vol.3 , pp. 300-313
    • Kirkwood, J.G.1
  • 33
    • 0034716751 scopus 로고    scopus 로고
    • A ligand that is predicted to bind better to avidin than biotin: Insights from computational fluorine scanning
    • Kuhn B, Kollman PA. 2000. A ligand that is predicted to bind better to avidin than biotin: insights from computational fluorine scanning. J. Am. Chem. Soc. 122: 3909-3916.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3909-3916
    • Kuhn, B.1    Kollman, P.A.2
  • 34
    • 0030466444 scopus 로고    scopus 로고
    • Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design
    • Ladbury JE. 1996. Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design. Chem. Biol. 3: 973-980.
    • (1996) Chem. Biol , vol.3 , pp. 973-980
    • Ladbury, J.E.1
  • 35
    • 33947418829 scopus 로고    scopus 로고
    • Proteinprotein recognition and interaction hot spots in an antigen-antibody complex: Free energy decomposition identifies ''efficient amino acids.'
    • Lafont V, Schaefer M, Stote RH, Altschuh D, Dejaegere A. 2007. Proteinprotein recognition and interaction hot spots in an antigen-antibody complex: free energy decomposition identifies ''efficient amino acids.'' Proteins 67: 418-434.
    • (2007) Proteins , vol.67 , pp. 418-434
    • Lafont, V.1    Schaefer, M.2    Stote, R.H.3    Altschuh, D.4    Dejaegere, A.5
  • 36
    • 0038792211 scopus 로고    scopus 로고
    • New analytic approximation to the standard molecular volume definition and its application to generalized Born calculations
    • Lee MS, Feig M, Salsbury FR, Jr Brooks CL, III. 2003. New analytic approximation to the standard molecular volume definition and its application to generalized Born calculations. J. Comput. Chem. 24: 1348-1356.
    • (2003) J. Comput. Chem. , vol.24 , pp. 1348-1356
    • Lee, M.S.1    Feig, M.2    Salsbury, F.R.3    Brooks Jr., C.L.4
  • 39
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons DS, Lieberman SA, Hampl J, Boniface JJ, Chien Y, Berg LJ, Davis MM. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 5: 53-61.
    • (1996) Immunity , vol.5 , pp. 53-61
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.5    Berg, L.J.6    Davis, M.M.7
  • 40
    • 0033568644 scopus 로고    scopus 로고
    • Computational alanine scanning to probe protein-protein interactions: A novel approach to evaluate binding free energies
    • Massova I, Kollman PA. 1999. Computational alanine scanning to probe protein-protein interactions: a novel approach to evaluate binding free energies. J. Am. Chem. Soc. 121: 8133-8143.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8133-8143
    • Massova, I.1    Kollman, P.A.2
  • 41
    • 34147133371 scopus 로고    scopus 로고
    • Recent developments in methodologies for calculating the entropy and free energy of biological systems by computer simulation
    • Meirovitch H. 2007. Recent developments in methodologies for calculating the entropy and free energy of biological systems by computer simulation. Curr. Opin. Struct. Biol. 17: 181-186.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 181-186
    • Meirovitch, H.1
  • 42
    • 34248137526 scopus 로고    scopus 로고
    • Combined simulation and mutagenesis analyses reveal the involvement of key residues for peroxisome proliferator-activated receptor alpha helix 12 dynamic behavior
    • Michalik L, Zoete V, Krey G, Grosdidier A, Gelman L, Chodanowski P, Feige JN, Desvergne B, Wahli W, Michielin O. 2007. Combined simulation and mutagenesis analyses reveal the involvement of key residues for peroxisome proliferator-activated receptor alpha helix 12 dynamic behavior. J. Biol. Chem. 282: 9666-9677.
    • (2007) J. Biol. Chem , vol.282 , pp. 9666-9677
    • Michalik, L.1    Zoete, V.2    Krey, G.3    Grosdidier, A.4    Gelman, L.5    Chodanowski, P.6    Feige, J.N.7    Desvergne, B.8    Wahli, W.9    Michielin, O.10
  • 43
    • 0036447407 scopus 로고    scopus 로고
    • Binding free energy differences in a TCR-peptide-MHC complex induced by a peptide mutation: A simulation analysis
    • Michielin O, Karplus M. 2002. Binding free energy differences in a TCR-peptide-MHC complex induced by a peptide mutation: a simulation analysis. J. Mol. Biol. 324: 547.
    • (2002) J. Mol. Biol. , vol.324 , pp. 547
    • Michielin, O.1    Karplus, M.2
  • 44
    • 33847650393 scopus 로고    scopus 로고
    • Computational alanine scanning mutagenesis-an improved methodological approach
    • Moreira IS, Fernandes PA, Ramos MJ. 2007. Computational alanine scanning mutagenesis-an improved methodological approach. J. Comp. Chem. 28: 644-654.
    • (2007) J. Comp. Chem , vol.28 , pp. 644-654
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 45
    • 33745467541 scopus 로고    scopus 로고
    • Unraveling the importance of protein-protein interaction: Application of a computational alanine-scanning mutagenesis to the study of the IgG1 streptococcal protein G (C2 fragment) complex
    • Moreira IS, Fernandes PA, Ramos MJ. 2006. Unraveling the importance of protein-protein interaction: application of a computational alanine-scanning mutagenesis to the study of the IgG1 streptococcal protein G (C2 fragment) complex. J. Phys. Chem. B 110: 10962-10969.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10962-10969
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 47
    • 28144441347 scopus 로고    scopus 로고
    • Evaluating the molecular mechanics poisson-boltzmann surface area free energy method using a congeneric series of ligands to p38 MAP kinase
    • Pearlman DA. 2005. Evaluating the molecular mechanics poisson-boltzmann surface area free energy method using a congeneric series of ligands to p38 MAP kinase. J. Med. Chem. 48: 7796-7807.
    • (2005) J. Med. Chem. , vol.48 , pp. 7796-7807
    • Pearlman, D.A.1
  • 56
    • 0032466648 scopus 로고    scopus 로고
    • Continuum solvent studies of the stability of RNA hairpin loops and helices
    • Srinivasan J, Miller J, Kollman PA, Case DA. 1998. Continuum solvent studies of the stability of RNA hairpin loops and helices. J. Biomol. Struct. Dyn. 16: 671-682.
    • (1998) J. Biomol. Struct. Dyn. , vol.16 , pp. 671-682
    • Srinivasan, J.1    Miller, J.2    Kollman, P.A.3    Case, D.A.4
  • 57
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still WC, Tempczyk A, Hawley RC, Hendrickson T. 1990. Semianalytical treatment of solvation for molecular mechanics and dynamics. J. Am. Chem. Soc. 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
  • 58
    • 5144220584 scopus 로고    scopus 로고
    • Crystal structure of the human lamin A coil 2B dimer: Implications for the head-to-tail association of nuclear lamins
    • Strelkov SV, Schumacher J, Burkhard P, Aebi U, Herrmann H. 2004. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 343: 1067-1080.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1067-1080
    • Strelkov, S.V.1    Schumacher, J.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 59
    • 0347949637 scopus 로고    scopus 로고
    • Revisiting free energy calculations: A theoretical connection to MM/PBSA and direct calculation of the association free energy
    • Swanson JM, Henchman RH, McCammon JA. 2004. Revisiting free energy calculations: a theoretical connection to MM/PBSA and direct calculation of the association free energy. Biophys. J. 86: 67-74.
    • (2004) Biophys. J , vol.86 , pp. 67-74
    • Swanson, J.M.1    Henchman, R.H.2    McCammon, J.A.3
  • 60
  • 61
    • 0028360307 scopus 로고
    • The contribution of vibrational entropy to molecular association
    • Tidor B, Karplus M. 1994. The contribution of vibrational entropy to molecular association. J. Mol. Biol. 238: 405-414.
    • (1994) J. Mol. Biol. , vol.238 , pp. 405-414
    • Tidor, B.1    Karplus, M.2
  • 63
    • 22544467432 scopus 로고    scopus 로고
    • Molecular basis of peptide recognition by the TCR: Affinity differences calculated using large scale computing
    • Wan S, Coveney PV, Flower DR. 2005. Molecular basis of peptide recognition by the TCR: affinity differences calculated using large scale computing. J. Immunol. 175: 1715-1723.
    • (2005) J. Immunol. , vol.175 , pp. 1715-1723
    • Wan, S.1    Coveney, P.V.2    Flower, D.R.3
  • 64
    • 33748339364 scopus 로고    scopus 로고
    • Structural assessment of single amino acid mutations: Application to TP53 function
    • Yip YL, Zoete V, Scheib H, Michielin O. 2006. Structural assessment of single amino acid mutations: application to TP53 function. Hum. Mutat. 27: 926-937.
    • (2006) Hum. Mutat , vol.27 , pp. 926-937
    • Yip, Y.L.1    Zoete, V.2    Scheib, H.3    Michielin, O.4
  • 65
    • 34248578077 scopus 로고    scopus 로고
    • Insights into unbinding mechanisms upon two mutations investigated by molecular dynamics study of GSK3beta-axin complex: Role of packing hydrophobic residues
    • Zhang N, Jiang Y, Zou J, Zhuang S, Jin H, Yu Q. 2007. Insights into unbinding mechanisms upon two mutations investigated by molecular dynamics study of GSK3beta-axin complex: role of packing hydrophobic residues. Proteins 67: 941-949.
    • (2007) Proteins , vol.67 , pp. 941-949
    • Zhang, N.1    Jiang, Y.2    Zou, J.3    Zhuang, S.4    Jin, H.5    Yu, Q.6
  • 68
    • 33750539273 scopus 로고    scopus 로고
    • Importance of individual side chains for the stability of a protein fold: Computational alanine scanning of the insulin monomer
    • Zoete V, Meuwly M. 2006. Importance of individual side chains for the stability of a protein fold: computational alanine scanning of the insulin monomer. J. Comput. Chem. 27: 1843-1857.
    • (2006) J. Comput. Chem. , vol.27 , pp. 1843-1857
    • Zoete, V.1    Meuwly, M.2
  • 69
    • 24344456625 scopus 로고    scopus 로고
    • Study of the insulin dimerization: Binding free energy calculations and per-residue free energy decomposition
    • Zoete V, Meuwly M, Karplus M. 2005. Study of the insulin dimerization: binding free energy calculations and per-residue free energy decomposition. Proteins 61: 79-93.
    • (2005) Proteins , vol.61 , pp. 79-93
    • Zoete, V.1    Meuwly, M.2    Karplus, M.3
  • 70
    • 34248562740 scopus 로고    scopus 로고
    • Comparison between computational alanine scanning and per-residue binding free energy decomposition for protein-protein association using MM-GBSA: Application to the TCR-p-MHC complex
    • Zoete V, Michielin O. 2007. Comparison between computational alanine scanning and per-residue binding free energy decomposition for protein-protein association using MM-GBSA: application to the TCR-p-MHC complex. Proteins 67: 1026-1047.
    • (2007) Proteins , vol.67 , pp. 1026-1047
    • Zoete, V.1    Michielin, O.2
  • 71
    • 36849122972 scopus 로고
    • High-temperature equation of state by a perturbation method I. Nonpolar gases
    • Zwanzig RW. 1954. High-temperature equation of state by a perturbation method I. Nonpolar gases. J. Chem. Phys. 22: 1420-1426.
    • (1954) J. Chem. Phys. , vol.22 , pp. 1420-1426
    • Zwanzig, R.W.1


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