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Volumn 60, Issue 3, 2011, Pages 283-295

Insights into the structure of the LC13 TCR/HLA-B8-EBV peptide complex with molecular dynamics simulations

Author keywords

turn; Epstein Barr virus; HLA B8; Molecular dynamics; pMHC TCR interactions; TCR interactions

Indexed keywords

HLA B8 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; PEPTIDE;

EID: 79958252468     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-011-9151-2     Document Type: Article
Times cited : (11)

References (66)
  • 2
    • 32544458887 scopus 로고    scopus 로고
    • T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3D structure-DB
    • Kaas, Q., & Lefranc, M. P. (2005). T cell receptor/peptide/MHC molecular characterization and standardized pMHC contact sites in IMGT/3D structure-DB. In Silico Biology, 5, 505-528.
    • (2005) In Silico Biology , vol.5 , pp. 505-528
    • Kaas, Q.1    Lefranc, M.P.2
  • 4
    • 47649130715 scopus 로고    scopus 로고
    • Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities
    • Armstrong, K. M., Insaidoo, F. K., & Baker, B. M. (2008). Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities. Journal of Molecular Recognition, 21, 275-287.
    • (2008) Journal of Molecular Recognition , vol.21 , pp. 275-287
    • Armstrong, K.M.1    Insaidoo, F.K.2    Baker, B.M.3
  • 5
    • 58149280299 scopus 로고    scopus 로고
    • T-cell receptor binding affinities and kinetics: Impact on T-cell activity and specificity
    • Stone, J. D., Chervin, A. S., & Kranz, D. M. (2009). T-cell receptor binding affinities and kinetics: Impact on T-cell activity and specificity. Immunology, 126, 165-176.
    • (2009) Immunology , vol.126 , pp. 165-176
    • Stone, J.D.1    Chervin, A.S.2    Kranz, D.M.3
  • 6
    • 0033118739 scopus 로고    scopus 로고
    • A kinetic basis for T cell receptor repertoire selection during an immune response
    • Savage, P. A., Boniface, J. J., & Davis, M. M. (1999). A kinetic basis for T cell receptor repertoire selection during an immune response. Immunity, 10, 485-492.
    • (1999) Immunity , vol.10 , pp. 485-492
    • Savage, P.A.1    Boniface, J.J.2    Davis, M.M.3
  • 7
    • 0031172162 scopus 로고    scopus 로고
    • Serial triggering of TCRs: A basis for the sensitivity and specificity of antigen recognition
    • Valitutti, S., & Lanzavecchia, A. (1997). Serial triggering of TCRs: A basis for the sensitivity and specificity of antigen recognition. Immunology Today, 18, 299-304.
    • (1997) Immunology Today , vol.18 , pp. 299-304
    • Valitutti, S.1    Lanzavecchia, A.2
  • 8
    • 0348047600 scopus 로고    scopus 로고
    • Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation
    • Krogsgaard, M., Prado, N., Adams, E. J., He, X., Chow, D. C., Wilson, D. B., et al. (2003). Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation. Molecular Cell, 12, 1367-1378.
    • (2003) Molecular Cell , vol.12 , pp. 1367-1378
    • Krogsgaard, M.1    Prado, N.2    Adams, E.J.3    He, X.4    Chow, D.C.5    Wilson, D.B.6    Garcia, K.C.7    Davis, M.M.8
  • 12
    • 0037343308 scopus 로고    scopus 로고
    • Molecular dynamics of biological macromolecules: A brief history and perspective
    • Karplus, M. (2003). Molecular dynamics of biological macromolecules: A brief history and perspective. Biopolymers, 68, 350-358.
    • (2003) Biopolymers , vol.68 , pp. 350-358
    • Karplus, M.1
  • 13
    • 39449116285 scopus 로고    scopus 로고
    • Biomolecular simulation: historical picture and future perspectives
    • van Gunsteren, W. F., & Dolenc, J. (2008). Biomolecular simulation: historical picture and future perspectives. Biochemical Society Transactions, 36, 11-15.
    • (2008) Biochemical Society Transactions , vol.36 , pp. 11-15
    • van Gunsteren, W.F.1    Dolenc, J.2
  • 15
    • 64049102289 scopus 로고    scopus 로고
    • Binding of small-molecule ligands to proteins: "what you see" is not always "what you get"
    • Mobley, D. L., & Dill, K. A. (2009). Binding of small-molecule ligands to proteins: "what you see" is not always "what you get". Structure, 17, 489-499.
    • (2009) Structure , vol.17 , pp. 489-499
    • Mobley, D.L.1    Dill, K.A.2
  • 17
    • 34248358109 scopus 로고    scopus 로고
    • Applications of Molecular Dynamics Simulations in immunology: A useful computational method in aiding vaccine design
    • Mallik, B., & Morikis, D. (2006). Applications of Molecular Dynamics Simulations in immunology: A useful computational method in aiding vaccine design. Current Proteomics, 3, 259-270.
    • (2006) Current Proteomics , vol.3 , pp. 259-270
    • Mallik, B.1    Morikis, D.2
  • 18
    • 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. Journal of Molecular Biology, 324, 547-569.
    • (2002) Journal of Molecular Biology , vol.324 , pp. 547-569
    • Michielin, O.1    Karplus, M.2
  • 19
    • 7644220670 scopus 로고    scopus 로고
    • Physical methods for structure, dynamics and binding in immunological research
    • Morikis, D., & Lambris, J. D. (2004). Physical methods for structure, dynamics and binding in immunological research. Trends in Immunology, 25, 700-707.
    • (2004) Trends in Immunology , vol.25 , pp. 700-707
    • Morikis, D.1    Lambris, J.D.2
  • 20
    • 58549110833 scopus 로고    scopus 로고
    • A disulfide linked model of the complement protein C8γ complexed with C8α indel peptide
    • Stavrakoudis, A. (2009). A disulfide linked model of the complement protein C8γ complexed with C8α indel peptide. Journal of Molecular Modeling, 15, 165-171.
    • (2009) Journal of Molecular Modeling , vol.15 , pp. 165-171
    • Stavrakoudis, A.1
  • 21
    • 78049512800 scopus 로고    scopus 로고
    • Conformational flexibility in designing peptides for immunology: The molecular dynamics approach
    • Stavrakoudis, A. (2010). Conformational flexibility in designing peptides for immunology: The molecular dynamics approach. Current Computer-Aided Drug Design, 6, 207-222.
    • (2010) Current Computer-Aided Drug Design , vol.6 , pp. 207-222
    • Stavrakoudis, A.1
  • 22
    • 37349112664 scopus 로고    scopus 로고
    • Toward an atomistic understanding of the immune synapse: large-scale molecular dynamics simulation of a membrane-embedded TCR-pMHC-CD4 complex
    • Wan, S., Flower, D. R., & Coveney, P. V. (2008). Toward an atomistic understanding of the immune synapse: large-scale molecular dynamics simulation of a membrane-embedded TCR-pMHC-CD4 complex. Molecular Immunology, 45, 1221-1230.
    • (2008) Molecular Immunology , vol.45 , pp. 1221-1230
    • Wan, S.1    Flower, D.R.2    Coveney, P.V.3
  • 23
    • 78149316174 scopus 로고    scopus 로고
    • T-cell epitope prediction and immune complex simulation using molecular dynamics: State of the art and persisting challenges
    • doi:10.1186/1745-7580-6-S2-S4
    • Flower, D. R., Phadwal, K., Macdonald, I. K., Coveney, P., Davies, M. N., & Wan, S. (2010). T-cell epitope prediction and immune complex simulation using molecular dynamics: State of the art and persisting challenges. Immunome Research, 6(Suppl 2), S4. doi: 10. 1186/1745-7580-6-S2-S4.
    • (2010) Immunome Research , vol.6 , Issue.SUPPL. 2
    • Flower, D.R.1    Phadwal, K.2    Macdonald, I.K.3    Coveney, P.4    Davies, M.N.5    Wan, S.6
  • 25
    • 56049117665 scopus 로고    scopus 로고
    • Protein-protein interaction investigated by steered molecular dynamics: The TCR-pMHC complex
    • Cuendet, M. A., & Michielin, O. (2008). Protein-protein interaction investigated by steered molecular dynamics: The TCR-pMHC complex. Biophysical Journal, 95, 3575-3590.
    • (2008) Biophysical Journal , vol.95 , pp. 3575-3590
    • Cuendet, M.A.1    Michielin, O.2
  • 26
    • 22544456941 scopus 로고    scopus 로고
    • Peptide recognition by the T cell receptor: Comparison of binding free energies from thermodynamic integration, Poisson-Boltzmann and linear interaction energy approximations
    • Wan, S., Coveney, P. V., & Flower, D. R. (2005). Peptide recognition by the T cell receptor: Comparison of binding free energies from thermodynamic integration, Poisson-Boltzmann and linear interaction energy approximations. Philosophical Transactions of the Royal Society A, 363, 2037-2053.
    • (2005) Philosophical Transactions of the Royal Society A , vol.363 , pp. 2037-2053
    • Wan, S.1    Coveney, P.V.2    Flower, D.R.3
  • 27
    • 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: Structure, Function, and Bioinformatics, 67, 1026-1047.
    • (2007) Proteins: Structure, Function, and Bioinformatics , vol.67 , pp. 1026-1047
    • Zoete, V.1    Michielin, O.2
  • 28
    • 76649121529 scopus 로고    scopus 로고
    • MM-GBSA binding free energy decomposition and T cell receptor engineering
    • Zoete, V., Irving, M. B., & Michielin, O. (2009). MM-GBSA binding free energy decomposition and T cell receptor engineering. Journal of Molecular Recognition, 23, 142-152.
    • (2009) Journal of Molecular Recognition , vol.23 , pp. 142-152
    • Zoete, V.1    Irving, M.B.2    Michielin, O.3
  • 30
    • 59449097827 scopus 로고    scopus 로고
    • Turns revisited: A uniform and comprehensive classification of normal, open, and reverse turn families minimizing unassigned random chain portions
    • Koch, O., & Klebe, G. (2009). Turns revisited: A uniform and comprehensive classification of normal, open, and reverse turn families minimizing unassigned random chain portions. Proteins: Structure, Function, and Bioinformatics, 74, 353-357.
    • (2009) Proteins: Structure, Function, and Bioinformatics , vol.74 , pp. 353-357
    • Koch, O.1    Klebe, G.2
  • 33
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S. E., & MacKerell, A. D., Jr. (2000). An improved empirical potential energy function for molecular simulations of phospholipids. The Journal of Physical Chemistry B, 104, 7510-7515.
    • (2000) The Journal of Physical Chemistry B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    Mackerell Jr., A.D.2
  • 34
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word, J. M., Lovell, S. C., Richardson, J. S., & Richardson, D. C. (1999). Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. Journal of Molecular Biology, 285, 1735-1747.
    • (1999) Journal of Molecular Biology , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 35
    • 0035526029 scopus 로고    scopus 로고
    • Structure and dynamics of the TIP3P, SPC, and SPC/E water models at 298 K
    • Mark, P., & Nilsson, L. (2001). Structure and dynamics of the TIP3P, SPC, and SPC/E water models at 298 K. The Journal of Physical Chemistry A, 105, 9954-9960.
    • (2001) The Journal of Physical Chemistry A , vol.105 , pp. 9954-9960
    • Mark, P.1    Nilsson, L.2
  • 36
    • 0343005873 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a polyalanine octapeptide under Ewald boundary conditions: influence of artificial periodicity on peptide conformation
    • Weber, W., Hunenberger, P. H., & McCammon, J. A. (2000). Molecular dynamics simulations of a polyalanine octapeptide under Ewald boundary conditions: influence of artificial periodicity on peptide conformation. The Journal of Physical Chemistry B, 104, 3668-3675.
    • (2000) The Journal of Physical Chemistry B , vol.104 , pp. 3668-3675
    • Weber, W.1    Hunenberger, P.H.2    McCammon, J.A.3
  • 37
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems
    • Darden, T., York, D., & Pedersen, L. (1993). Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems. Journal of Chemical Physics, 98, 10089-11092.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 10089-11092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 38
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., Ciccotti, G., & Berendsen, H. J. C. (1977). Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. Journal of Computational Physics, 23, 327-341.
    • (1977) Journal of Computational Physics , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 40
    • 78650722548 scopus 로고    scopus 로고
    • Eucb: A C++ program for molecular dynamics trajectory analysis
    • Tsoulos, I. G., & Stavrakoudis, A. (2011). Eucb: A C++ program for molecular dynamics trajectory analysis. Computer Physics Communications, 182, 834-841.
    • (2011) Computer Physics Communications , vol.182 , pp. 834-841
    • Tsoulos, I.G.1    Stavrakoudis, A.2
  • 42
    • 0021203270 scopus 로고
    • A comparison of several "single-pass" estimators of the standard deviation of wind direction
    • Yamartino, R. J. (1984). A comparison of several "single-pass" estimators of the standard deviation of wind direction. Journal of Climate and Applied Meteorology, 23, 1362-1366.
    • (1984) Journal of Climate and Applied Meteorology , vol.23 , pp. 1362-1366
    • Yamartino, R.J.1
  • 43
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson, E. G., & Thornton, J. M. (1994). A revised set of potentials for beta-turn formation in proteins. Protein Science, 3, 2207-22016.
    • (1994) Protein Science , vol.3 , pp. 2207-22016
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 44
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turn in proteins
    • Wilmot, C. M., & Thornton, J. M. (1988). Analysis and prediction of the different types of β-turn in proteins. Journal of Molecular Biology, 203, 221-232.
    • (1988) Journal of Molecular Biology , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 45
    • 33749172039 scopus 로고    scopus 로고
    • Carma: A molecular dynamics analysis program
    • Glykos, N. M. (2006). Carma: A molecular dynamics analysis program. Journal of Computational Chemistry, 27, 1765-1768.
    • (2006) Journal of Computational Chemistry , vol.27 , pp. 1765-1768
    • Glykos, N.M.1
  • 47
    • 0001351515 scopus 로고
    • Estimation of absolute and relative entropies of macromolecules using the covariance matrix
    • Schlitter, J. (1993). Estimation of absolute and relative entropies of macromolecules using the covariance matrix. Chemical Physics Letters, 215, 617-621.
    • (1993) Chemical Physics Letters , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 48
    • 0035828630 scopus 로고    scopus 로고
    • On the calculation of entropy from covariance matrices of the atomic fluctuations
    • Andricioaei, I., & Karplus, M. (2001). On the calculation of entropy from covariance matrices of the atomic fluctuations. The Journal of Chemical Physics, 115, 6289.
    • (2001) The Journal of Chemical Physics , vol.115 , pp. 6289
    • Andricioaei, I.1    Karplus, M.2
  • 49
    • 33645786604 scopus 로고    scopus 로고
    • Importance of the CMAP correction to the CHARMM22 protein force field: Dynamics of hen lysozyme
    • Buck, M., Bouguet-Bonnet, S., Pastor, R. W., & MacKerell, A. D., Jr. (2006). Importance of the CMAP correction to the CHARMM22 protein force field: Dynamics of hen lysozyme. Biophysical Journal, 90, 36-38.
    • (2006) Biophysical Journal , vol.90 , pp. 36-38
    • Buck, M.1    Bouguet-Bonnet, S.2    Pastor, R.W.3    Mackerell Jr., A.D.4
  • 50
    • 48749111845 scopus 로고    scopus 로고
    • Molecular dynamics simulations of an apoliprotein derived peptide
    • Stavrakoudis, A. (2008). Molecular dynamics simulations of an apoliprotein derived peptide. Chemical Physics Letters, 461, 294-299.
    • (2008) Chemical Physics Letters , vol.461 , pp. 294-299
    • Stavrakoudis, A.1
  • 51
    • 10844292652 scopus 로고    scopus 로고
    • Energy landscape of a small peptide revealed by dihedral angle principal component analysis
    • Mu, Y., Nguyen, P. H., & Stock, G. (2005). Energy landscape of a small peptide revealed by dihedral angle principal component analysis. Proteins: Structure, Function, and Bioinformatics, 58, 45-52.
    • (2005) Proteins: Structure, Function, and Bioinformatics , vol.58 , pp. 45-52
    • Mu, Y.1    Nguyen, P.H.2    Stock, G.3
  • 52
    • 73949118375 scopus 로고    scopus 로고
    • Molecular Dynamics simulations of BcZBP, a deacetylase from bacillus cereus: active site loops determine substrate accessibility and specificity
    • Fadouloglou, V. E., Stavrakoudis, A., Bouriotis, V., Kokkinidis, M., & Glykos, N. M. (2009). Molecular Dynamics simulations of BcZBP, a deacetylase from bacillus cereus: active site loops determine substrate accessibility and specificity. The Journal of Chemical Theory and Computation, 5, 3299-3311.
    • (2009) The Journal of Chemical Theory and Computation , vol.5 , pp. 3299-3311
    • Fadouloglou, V.E.1    Stavrakoudis, A.2    Bouriotis, V.3    Kokkinidis, M.4    Glykos, N.M.5
  • 57
    • 58849111704 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the TSSPSAD Peptide Antigen in free and bound with CAMPATH-1H Fab antibody states: the importance of the β-turn conformation
    • Tatsis, V. A., Tsoulos, I. G., & Stavrakoudis, A. (2009). Molecular dynamics simulations of the TSSPSAD Peptide Antigen in free and bound with CAMPATH-1H Fab antibody states: the importance of the β-turn conformation. International Journal of Peptide Research and Therapeutics, 15, 1-9.
    • (2009) International Journal of Peptide Research and Therapeutics , vol.15 , pp. 1-9
    • Tatsis, V.A.1    Tsoulos, I.G.2    Stavrakoudis, A.3
  • 58
    • 34249061686 scopus 로고    scopus 로고
    • On the application of molecular-dynamics simulations to validate thermal parameters and to optimize TLS-group selection for macromolecular refinement
    • Glykos, N. (2007). On the application of molecular-dynamics simulations to validate thermal parameters and to optimize TLS-group selection for macromolecular refinement. Acta Crystallographica Section D, D63, 705-713.
    • (2007) Acta Crystallographica Section D , vol.D63 , pp. 705-713
    • Glykos, N.1
  • 59
    • 0030961098 scopus 로고    scopus 로고
    • Backbone entropy of loops as a measure of their flexibility: application to a ras protein simulated by molecular dynamics
    • Meirovitch, H., & Hendrickson, T. F. (1997). Backbone entropy of loops as a measure of their flexibility: application to a ras protein simulated by molecular dynamics. Proteins: Structure, Function, and Bioinformatics, 29, 127-140.
    • (1997) Proteins: Structure, Function, and Bioinformatics , vol.29 , pp. 127-140
    • Meirovitch, H.1    Hendrickson, T.F.2
  • 60
    • 54049111388 scopus 로고    scopus 로고
    • Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes
    • Armstrong, K. M., Piepenbrink, K. H., & Baker, B. M. (2008). Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Biochemical Journal, 415, 183-196.
    • (2008) Biochemical Journal , vol.415 , pp. 183-196
    • Armstrong, K.M.1    Piepenbrink, K.H.2    Baker, B.M.3
  • 61
    • 0036839356 scopus 로고    scopus 로고
    • The structure of HLA-B8 complexed to an immunodominant viral determinant: Peptide-induced conformational changes and a mode of MHC class I dimerization
    • Kjer-Nielsen, L., Clements, C. S., Brooks, A. G., Purcell, A. W., Fontes, M., McCluskey, J., et al. (2002). The structure of HLA-B8 complexed to an immunodominant viral determinant: Peptide-induced conformational changes and a mode of MHC class I dimerization. The Journal of Immunology, 169, 5153-5160.
    • (2002) The Journal of Immunology , vol.169 , pp. 5153-5160
    • Kjer-Nielsen, L.1    Clements, C.S.2    Brooks, A.G.3    Purcell, A.W.4    Fontes, M.5    McCluskey, J.6    Rossjohn, J.7
  • 62
    • 38949100462 scopus 로고    scopus 로고
    • The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vβ domain
    • Ishizuka, J., Stewart-Jones, G. B. E., van der Merwe, A., Bell, J. I., McMichael, A. J., & Jones, E. Y. (2008). The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vβ domain. Immunity, 28, 171-182.
    • (2008) Immunity , vol.28 , pp. 171-182
    • Ishizuka, J.1    Stewart-Jones, G.B.E.2    van der Merwe, A.3    Bell, J.I.4    McMichael, A.J.5    Jones, E.Y.6
  • 64
    • 1842534583 scopus 로고    scopus 로고
    • MHC-peptide binding is assisted by bound water molecules
    • Petrone, P. M., & Garcia, A. E. (2004). MHC-peptide binding is assisted by bound water molecules. Journal of Molecular Biology, 338, 419-435.
    • (2004) Journal of Molecular Biology , vol.338 , pp. 419-435
    • Petrone, P.M.1    Garcia, A.E.2
  • 65
    • 0021470624 scopus 로고
    • Buried surface area conformational entropy, and protein stability
    • Rashin, A. (1984). Buried surface area conformational entropy, and protein stability. Biopolymers, 23, 1605-1620.
    • (1984) Biopolymers , vol.23 , pp. 1605-1620
    • Rashin, A.1
  • 66
    • 65249187243 scopus 로고    scopus 로고
    • MM-PBSA captures key role of intercalating water molecules at a protein-protein interface
    • Wong, S., Amaro, R. E., & McCammon, J. A. (2009). MM-PBSA captures key role of intercalating water molecules at a protein-protein interface. The Journal of Chemical Theory and Computation, 5, 422-429.
    • (2009) The Journal of Chemical Theory and Computation , vol.5 , pp. 422-429
    • Wong, S.1    Amaro, R.E.2    McCammon, J.A.3


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