메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Activation of G-protein-coupled receptors correlates with the formation of a continuous internal water pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; G PROTEIN COUPLED RECEPTOR; TYROSINE; WATER; ADENOSINE A2A RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; RHODOPSIN;

EID: 84921026921     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5733     Document Type: Article
Times cited : (192)

References (56)
  • 1
    • 79960979207 scopus 로고    scopus 로고
    • Proton transfer via a transient linear water-molecule chain in a membrane protein
    • Freier, E., Wolf, S. & Gerwert, K. Proton transfer via a transient linear water-molecule chain in a membrane protein. Proc. Natl Acad. Sci. USA 108, 11435-11439 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 11435-11439
    • Freier, E.1    Wolf, S.2    Gerwert, K.3
  • 2
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • Venkatakrishnan, A. J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185-194 (2013).
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1
  • 3
    • 79956305477 scopus 로고    scopus 로고
    • Role of bulk water in hydrolysis of the rhodopsin chromophore
    • Jastrzebska, B., Palczewski, K. & Golczak, M. Role of bulk water in hydrolysis of the rhodopsin chromophore. J. Biol. Chem. 286, 18930-18937 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 18930-18937
    • Jastrzebska, B.1    Palczewski, K.2    Golczak, M.3
  • 4
    • 66649096395 scopus 로고    scopus 로고
    • Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G proteincoupled receptors
    • Angel, T. E., Chance, M. R. & Palczewski, K. Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G proteincoupled receptors. Proc. Natl Acad. Sci. USA 106, 8555-8560 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8555-8560
    • Angel, T.E.1    Chance, M.R.2    Palczewski, K.3
  • 5
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the b2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. F. et al. Crystal structure of the b2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.F.1
  • 6
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • Choe, H. W. et al. Crystal structure of metarhodopsin II. Nature 471, 651-655 (2011).
    • (2011) Nature , vol.471 , pp. 651-655
    • Choe, H.W.1
  • 7
    • 84861961427 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of GPCRs by sodium ions
    • Liu, W. et al. Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions. Science 337, 232-236 (2012).
    • (2012) Science , vol.337 , pp. 232-236
    • Liu, W.1
  • 8
    • 84884237285 scopus 로고    scopus 로고
    • The role of water and sodium ions in the activation of the m-opioid receptor
    • Yuan, S., Vogel, H. & Filipek, S. The role of water and sodium ions in the activation of the m-opioid receptor. Angew. Chem. 52, 10112-10115 (2013).
    • (2013) Angew. Chem. , vol.52 , pp. 10112-10115
    • Yuan, S.1    Vogel, H.2    Filipek, S.3
  • 9
    • 84856156564 scopus 로고    scopus 로고
    • Prediction of a ligand-binding niche within a human olfactory receptor by combining sitedirected mutagenesis with dynamic homology modeling
    • Gelis, L., Wolf, S., Hatt, H., Neuhaus, E. M. & Gerwert, K. Prediction of a ligand-binding niche within a human olfactory receptor by combining sitedirected mutagenesis with dynamic homology modeling. Angew. Chem. Int. Ed. 51, 1274-1278 (2012).
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 1274-1278
    • Gelis, L.1    Wolf, S.2    Hatt, H.3    Neuhaus, E.M.4    Gerwert, K.5
  • 10
    • 47749099638 scopus 로고    scopus 로고
    • Mechanism of signal propagation upon retinal isomerization: Insights from molecular dynamics simulations of rhodopsin restrained by normal modes
    • Isin, B., Schulten, K., Tajkhorshid, E. & Bahar, I. Mechanism of signal propagation upon retinal isomerization: Insights from molecular dynamics simulations of rhodopsin restrained by normal modes. Biophys. J. 95, 789-803 (2008).
    • (2008) Biophys. J. , vol.95 , pp. 789-803
    • Isin, B.1    Schulten, K.2    Tajkhorshid, E.3    Bahar, I.4
  • 11
    • 34247847854 scopus 로고    scopus 로고
    • The signaling pathway of rhodopsin
    • Kong, Y. F. & Karplus, M. The signaling pathway of rhodopsin. Structure 15, 611-623 (2007).
    • (2007) Structure , vol.15 , pp. 611-623
    • Kong, Y.F.1    Karplus, M.2
  • 12
    • 84893954062 scopus 로고    scopus 로고
    • Molecular control of d-opioid receptor signalling
    • Fenalti, G. et al. Molecular control of d-opioid receptor signalling. Nature 506, 191-196 (2014).
    • (2014) Nature , vol.506 , pp. 191-196
    • Fenalti, G.1
  • 13
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • Lebon, G. et al. Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 474, 521-525 (2011).
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1
  • 14
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T. et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342, 571-583 (2004).
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1
  • 15
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss, J. et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471, 656-660 (2011).
    • (2011) Nature , vol.471 , pp. 656-660
    • Standfuss, J.1
  • 16
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human b2-adrenergic G protein-coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human b2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 17
    • 63849294621 scopus 로고    scopus 로고
    • Identification of two distinct inactive conformations of the b2-adrenergic receptor reconciles structural and biochemical observations
    • Dror, R. O. et al. Identification of two distinct inactive conformations of the b2-adrenergic receptor reconciles structural and biochemical observations. Proc. Natl Acad. Sci. USA 106, 4689-4694 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4689-4694
    • Dror, R.O.1
  • 18
    • 84877631485 scopus 로고    scopus 로고
    • Structural features for functional selectivity at serotonin receptors
    • Wacker, D. et al. Structural features for functional selectivity at serotonin receptors. Science 340, 615-619 (2013).
    • (2013) Science , vol.340 , pp. 615-619
    • Wacker, D.1
  • 19
    • 84873298278 scopus 로고    scopus 로고
    • The dynamic process of b2-adrenergic receptor activation
    • Nygaard, R. et al. The dynamic process of b2-adrenergic receptor activation. Cell 152, 532-542 (2013).
    • (2013) Cell , vol.152 , pp. 532-542
    • Nygaard, R.1
  • 20
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 21
    • 84878906754 scopus 로고    scopus 로고
    • Ligand-dependent activation and deactivation of the human adenosine A2A receptor
    • Li, J., Jonsson, A. L., Beuming, T., Shelley, J. C. & Voth, G. A. Ligand-dependent activation and deactivation of the human adenosine A2A receptor. J. Am. Chem. Soc. 135, 8749-8759 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8749-8759
    • Li, J.1    Jonsson, A.L.2    Beuming, T.3    Shelley, J.C.4    Voth, G.A.5
  • 22
    • 84858164791 scopus 로고    scopus 로고
    • Action of molecular switches in GPCRs-theoretical and experimental studies
    • Trzaskowski, B. et al. Action of molecular switches in GPCRs-theoretical and experimental studies. Curr. Med. Chem. 19, 1090-1109 (2012).
    • (2012) Curr. Med. Chem. , vol.19 , pp. 1090-1109
    • Trzaskowski, B.1
  • 23
    • 0035980071 scopus 로고    scopus 로고
    • Arrestin specificity for G protein-coupled receptors in human airway smooth muscle
    • Penn, R. B. et al. Arrestin specificity for G protein-coupled receptors in human airway smooth muscle. J. Biol. Chem. 276, 32648-32656 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 32648-32656
    • Penn, R.B.1
  • 24
    • 81755163613 scopus 로고    scopus 로고
    • Activation mechanism of the b2-adrenergic receptor
    • Dror, R. O. et al. Activation mechanism of the b2-adrenergic receptor. Proc. Natl Acad. Sci. USA 108, 18684-18689 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 18684-18689
    • Dror, R.O.1
  • 25
    • 84877607189 scopus 로고    scopus 로고
    • Structural basis for molecular recognition at serotonin receptors
    • Wang, C. et al. Structural basis for molecular recognition at serotonin receptors. Science 340, 610-614 (2013).
    • (2013) Science , vol.340 , pp. 610-614
    • Wang, C.1
  • 26
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: A site-directed spinlabeling study
    • Altenbach, C. et al. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spinlabeling study. Biochemistry 35, 12470-12478 (1996).
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1
  • 27
    • 0029730779 scopus 로고    scopus 로고
    • Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant
    • Han, M., Lin, S. W., Minkova, M., Smith, S. O. & Sakmar, T. P. Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant. J. Biol. Chem. 271, 32337-32342 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 32337-32342
    • Han, M.1    Lin, S.W.2    Minkova, M.3    Smith, S.O.4    Sakmar, T.P.5
  • 28
    • 84885448271 scopus 로고    scopus 로고
    • Opsin, a structural model for olfactory receptors?
    • Park, J. H. et al. Opsin, a structural model for olfactory receptors? Angew. Chem. 52, 11021-11024 (2013).
    • (2013) Angew. Chem. , vol.52 , pp. 11021-11024
    • Park, J.H.1
  • 29
    • 84869987897 scopus 로고    scopus 로고
    • The role of water in activation mechanism of human N-formyl Peptide Receptor 1 (FPR1) based on molecular dynamics simulations
    • Yuan, S. et al. The role of water in activation mechanism of human N-formyl Peptide Receptor 1 (FPR1) based on molecular dynamics simulations. PLoS ONE 7, e47114 (2012).
    • (2012) PLoS ONE , vol.7
    • Yuan, S.1
  • 30
    • 84887294827 scopus 로고    scopus 로고
    • Lipid receptor S1P1 activation scheme concluded from microsecond all-atom molecular dynamics simulations
    • Yuan, S., Wu, R., Latek, D., Trzaskowski, B. & Filipek, S. Lipid receptor S1P1 activation scheme concluded from microsecond all-atom molecular dynamics simulations. PLoS Comput. Biol. 9, e1003261 (2013).
    • (2013) PLoS Comput. Biol. , vol.9
    • Yuan, S.1    Wu, R.2    Latek, D.3    Trzaskowski, B.4    Filipek, S.5
  • 31
    • 48849113878 scopus 로고    scopus 로고
    • Comparative protein structure modeling using MODELLER
    • Unit 2 9
    • Eswar, N. et al. Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. Chapter 2, Unit 2 9 (2007).
    • (2007) Curr. Protoc. Protein Sci. Chapter , vol.2
    • Eswar, N.1
  • 32
    • 68349104348 scopus 로고    scopus 로고
    • Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling
    • Mandell, D. J., Coutsias, E. A. & Kortemme, T. Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling. Nat. Methods 6, 551-552 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 551-552
    • Mandell, D.J.1    Coutsias, E.A.2    Kortemme, T.3
  • 33
    • 79960258119 scopus 로고    scopus 로고
    • Improved treatment of ligands and coupling effects in empirical calculation and rationalization of pK(a) values
    • Sondergaard, C. R., Olsson, M. H. M., Rostkowski, M. & Jensen, J. H. Improved treatment of ligands and coupling effects in empirical calculation and rationalization of pK(a) values. J. Chem. Theory Comput. 7, 2284-2295 (2011).
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 2284-2295
    • Sondergaard, C.R.1    Olsson, M.H.M.2    Rostkowski, M.3    Jensen, J.H.4
  • 34
    • 0031019660 scopus 로고    scopus 로고
    • Opioid receptorcoupled G-proteins in rat locus coeruleus membranes: Decrease in activity after chronic morphine treatment
    • Selley, D. E., Nestler, E. J., Breivogel, C. S. & Childers, S. R. Opioid receptorcoupled G-proteins in rat locus coeruleus membranes: decrease in activity after chronic morphine treatment. Brain Res. 746, 10-18 (1997).
    • (1997) Brain Res. , vol.746 , pp. 10-18
    • Selley, D.E.1    Nestler, E.J.2    Breivogel, C.S.3    Childers, S.R.4
  • 35
    • 0030846678 scopus 로고    scopus 로고
    • In vitro autoradiographic localization of 5-HT1A receptor-activated G-proteins in the rat brain
    • Sim, L. J., Xiao, R. & Childers, S. R. In vitro autoradiographic localization of 5-HT1A receptor-activated G-proteins in the rat brain. Brain Res. Bull. 44, 39-45 (1997).
    • (1997) Brain Res. Bull. , vol.44 , pp. 39-45
    • Sim, L.J.1    Xiao, R.2    Childers, S.R.3
  • 36
    • 84861400021 scopus 로고    scopus 로고
    • Pubchem's bioassay database
    • Wang, Y. L. et al. Pubchem's bioassay database. Nucleic Acids Res. 40, D400-D412 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. D400-D412
    • Wang, Y.L.1
  • 37
    • 77955709186 scopus 로고    scopus 로고
    • Towards the comprehensive, rapid, and accurate prediction of the favorable tautomeric states of drug-like molecules in aqueous solution
    • Greenwood, J. R., Calkins, D., Sullivan, A. P. & Shelley, J. C. Towards the comprehensive, rapid, and accurate prediction of the favorable tautomeric states of drug-like molecules in aqueous solution. J. Comput. Aided Mol. Des. 24, 591-604 (2010).
    • (2010) J. Comput. Aided Mol. Des. , vol.24 , pp. 591-604
    • Greenwood, J.R.1    Calkins, D.2    Sullivan, A.P.3    Shelley, J.C.4
  • 38
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • Halgren, T. A. et al. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J. Med. Chem. 47, 1750-1759 (2004).
    • (2004) J. Med. Chem. , vol.47 , pp. 1750-1759
    • Halgren, T.A.1
  • 39
    • 12144289984 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner, R. A. et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J. Med. Chem. 47, 1739-1749 (2004).
    • (2004) J. Med. Chem , vol.47 , pp. 1739-1749
    • Friesner, R.A.1
  • 40
    • 77954256616 scopus 로고    scopus 로고
    • G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
    • Wolf, M. G., Hoefling, M., Aponte-Santamaria, C., Grubmuller, H. & Groenhof, G. g-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation. J. Comput. Chem. 31, 2169-2174 (2010).
    • (2010) J. Comput. Chem. , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaria, C.3    Grubmuller, H.4    Groenhof, G.5
  • 41
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk, S. et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29, 845-854 (2013).
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1
  • 42
    • 79955406829 scopus 로고    scopus 로고
    • Anisotropic solvent model of the lipid bilayer. 1. Parameterization of long-range electrostatics and first solvation shell effects
    • Lomize, A. L., Pogozheva, I. D. & Mosberg, H. I. Anisotropic solvent model of the lipid bilayer. 1. Parameterization of long-range electrostatics and first solvation shell effects. J. Chem. Inf. Model. 51, 918-929 (2011).
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 918-929
    • Lomize, A.L.1    Pogozheva, I.D.2    Mosberg, H.I.3
  • 43
    • 79955409906 scopus 로고    scopus 로고
    • Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes
    • Lomize, A. L., Pogozheva, I. D. & Mosberg, H. I. Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes. J. Chem. Inf. Model. 51, 930-946 (2011).
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 930-946
    • Lomize, A.L.1    Pogozheva, I.D.2    Mosberg, H.I.3
  • 44
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Lindorff-Larsen, K. et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78, 1950-1958 (2010).
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1
  • 45
    • 84858321169 scopus 로고    scopus 로고
    • Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids
    • Jambeck, J. P. M. & Lyubartsev, A. P. Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids. J. Phys. Chem. B 116, 3164-3179 (2012).
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3164-3179
    • Jambeck, J.P.M.1    Lyubartsev, A.P.2
  • 46
    • 84865101970 scopus 로고    scopus 로고
    • An extension and further validation of an all-atomistic force field for biological membranes
    • Jambeck, J. P. M. & Lyubartsev, A. P. An extension and further validation of an all-atomistic force field for biological membranes. J. Chem. Theory Comput. 8, 2938-2948 (2012).
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 2938-2948
    • Jambeck, J.P.M.1    Lyubartsev, A.P.2
  • 47
    • 79958841703 scopus 로고    scopus 로고
    • SwissParam: A fast force field generation tool for small organic molecules
    • Zoete, V., Cuendet, M. A., Grosdidier, A. & Michielin, O. SwissParam: a fast force field generation tool for small organic molecules. J. Comput. Chem. 32, 2359-2368 (2011).
    • (2011) J. Comput. Chem. , vol.32 , pp. 2359-2368
    • Zoete, V.1    Cuendet, M.A.2    Grosdidier, A.3    Michielin, O.4
  • 48
    • 80053102933 scopus 로고    scopus 로고
    • Time-resolved WAXS reveals accelerated conformational changes in iodoretinal-substituted proteorhodopsin
    • Malmerberg, E. et al. Time-resolved WAXS reveals accelerated conformational changes in iodoretinal-substituted proteorhodopsin. Biophys. J. 101, 1345-1353 (2011).
    • (2011) Biophys. J. , vol.101 , pp. 1345-1353
    • Malmerberg, E.1
  • 51
    • 69349100797 scopus 로고    scopus 로고
    • PLUMED: A portable plugin for free-energy calculations with molecular dynamics
    • Bonomi, M. et al. PLUMED: A portable plugin for free-energy calculations with molecular dynamics. Comput. Phys. Commun. 180, 1961-1972 (2009).
    • (2009) Comput. Phys. Commun. , vol.180 , pp. 1961-1972
    • Bonomi, M.1
  • 52
    • 38349091489 scopus 로고    scopus 로고
    • Well-tempered metadynamics: A smoothly converging and tunable free-energy method
    • Barducci, A., Bussi, G. & Parrinello, M. Well-tempered metadynamics: A smoothly converging and tunable free-energy method. Phys. Rev. Lett. 100, 020603 (2008).
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 020603
    • Barducci, A.1    Bussi, G.2    Parrinello, M.3
  • 53
    • 79953862815 scopus 로고    scopus 로고
    • Mechanism of membrane curvature sensing by amphipathic helix containing proteins
    • Cui, H. S., Lyman, E. & Voth, G. A. Mechanism of membrane curvature sensing by amphipathic helix containing proteins. Biophys. J. 100, 1271-1279 (2011).
    • (2011) Biophys. J. , vol.100 , pp. 1271-1279
    • Cui, H.S.1    Lyman, E.2    Voth, G.A.3
  • 54
    • 67650477115 scopus 로고    scopus 로고
    • Reconstructing the equilibrium Boltzmann distribution from well-tempered metadynamics
    • Bonomi, M., Barducci, A. & Parrinello, M. Reconstructing the equilibrium Boltzmann distribution from well-tempered metadynamics. J. Comput. Chem. 30, 1615-1621 (2009).
    • (2009) J. Comput. Chem. , vol.30 , pp. 1615-1621
    • Bonomi, M.1    Barducci, A.2    Parrinello, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.