메뉴 건너뛰기




Volumn 106, Issue 28, 2009, Pages 11576-11581

Functional implications of multistage copper binding to the prion protein

Author keywords

Copper attachment; Hybrid DFT; Metalloprotein; Misfolding; Neurodegenerative diseases

Indexed keywords

COPPER ION; HISTIDINE; IMIDAZOLE; NITROGEN; PRION PROTEIN;

EID: 67650860462     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0903807106     Document Type: Article
Times cited : (35)

References (62)
  • 1
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner S (1997) Prion diseases and the BSE crisis. Science 278:245-251.
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.1
  • 3
    • 0033570367 scopus 로고    scopus 로고
    • Evidence of presynaptic location and function of the prion protein
    • Herms J, et al. (1999) Evidence of presynaptic location and function of the prion protein. J Neurosci 19:8866-8875.
    • (1999) J Neurosci , vol.19 , pp. 8866-8875
    • Herms, J.1
  • 4
    • 0031080867 scopus 로고    scopus 로고
    • Prion protein and the transmissible spongiform encephalopathies
    • Caughey B, Chesebro B (1997) Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol 7:56-62.
    • (1997) Trends Cell Biol , vol.7 , pp. 56-62
    • Caughey, B.1    Chesebro, B.2
  • 5
    • 33845641044 scopus 로고    scopus 로고
    • Structure, function, and amyloidogenesis of fungal prions: Filament polymorphism and prion variants
    • Baxa U, Cassese T, Kajava A, Steven A (2006) Structure, function, and amyloidogenesis of fungal prions: Filament polymorphism and prion variants. Adv Protein Chem 73:125-180.
    • (2006) Adv Protein Chem , vol.73 , pp. 125-180
    • Baxa, U.1    Cassese, T.2    Kajava, A.3    Steven, A.4
  • 6
    • 0028844207 scopus 로고
    • Copper-binding to the n-terminal tandem repeat region of mammalian and avian prion protein-Structural studies using synthetic peptides
    • Hornshaw MP, Mcdermott JR, Candy JM, Lakey JH (1995) Copper-binding to the n-terminal tandem repeat region of mammalian and avian prion protein-Structural studies using synthetic peptides. Biochem Bioph Res Commun 214:993-999.
    • (1995) Biochem Bioph Res Commun , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    Mcdermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 7
    • 0028883341 scopus 로고
    • Copper-binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • Hornshaw MP, Mcdermott JR, Candy JM (1995) Copper-binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem Bioph Res Commun 207:621-629.
    • (1995) Biochem Bioph Res Commun , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    Mcdermott, J.R.2    Candy, J.M.3
  • 8
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown D, et al. (1997) The cellular prion protein binds copper in vivo. Nature 390:684-687.
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.1
  • 9
    • 0035873869 scopus 로고    scopus 로고
    • Imbalance of antioxidant defense in mice lacking cellular prion protein
    • Klamt F, et al. (2001) Imbalance of antioxidant defense in mice lacking cellular prion protein. Free Radical Biol Med 30:1137-1144.
    • (2001) Free Radical Biol Med , vol.30 , pp. 1137-1144
    • Klamt, F.1
  • 10
    • 0041302374 scopus 로고    scopus 로고
    • Cellular prion protein function in copper homeostasis and redox signalling at the synapse
    • Vassallo N, Herms J (2003) Cellular prion protein function in copper homeostasis and redox signalling at the synapse. J Neurochem 86:538-544.
    • (2003) J Neurochem , vol.86 , pp. 538-544
    • Vassallo, N.1    Herms, J.2
  • 11
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • Rachidi W, et al. (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J Biol Chem 278:9064-9072.
    • (2003) J Biol Chem , vol.278 , pp. 9064-9072
    • Rachidi, W.1
  • 12
    • 0037316675 scopus 로고    scopus 로고
    • Tethering the N-terminus of the prion protein compromises the cellular response to oxidative stress
    • Zeng FN, Watt NT, Walmsley AR, Hooper NM (2003) Tethering the N-terminus of the prion protein compromises the cellular response to oxidative stress. J Neurochem 84:480-490.
    • (2003) J Neurochem , vol.84 , pp. 480-490
    • Zeng, F.N.1    Watt, N.T.2    Walmsley, A.R.3    Hooper, N.M.4
  • 13
    • 0033571055 scopus 로고    scopus 로고
    • Normal prion protein has an activity like that of superoxide dismutase
    • Brown DR, et al. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem J 344:1-5.
    • (1999) Biochem J , vol.344 , pp. 1-5
    • Brown, D.R.1
  • 14
    • 0033996803 scopus 로고    scopus 로고
    • Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry
    • Whittal R, Ball H, Cohen F, Prusiner A, Baldwin M (2000) Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry. Protein Sci 9:332-343.
    • (2000) Protein Sci , vol.9 , pp. 332-343
    • Whittal, R.1    Ball, H.2    Cohen, F.3    Prusiner, A.4    Baldwin, M.5
  • 15
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P, Harris D (1998) Copper stimulates endocytosis of the prion protein. J Biol Chem 273:33107-33110.
    • (1998) J Biol Chem , vol.273 , pp. 33107-33110
    • Pauly, P.1    Harris, D.2
  • 16
    • 18344369706 scopus 로고    scopus 로고
    • Molecular features of the copper binding sites in the octarepeat domain of the prion protein
    • Burns CS, et al. (2002) Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry 41:3991-4001.
    • (2002) Biochemistry , vol.41 , pp. 3991-4001
    • Burns, C.S.1
  • 17
    • 0034649237 scopus 로고    scopus 로고
    • Identification of the Cu 2 binding sites in the Nterminal domain of the prion protein by EPR and CD spectroscopy
    • Aronoff-Spencer E, et al. (2000) Identification of the Cu 2 binding sites in the Nterminal domain of the prion protein by EPR and CD spectroscopy. Biochemistryistry 39:13760-13771.
    • (2000) Biochemistryistry , vol.39 , pp. 13760-13771
    • Aronoff-Spencer, E.1
  • 18
    • 0037646939 scopus 로고    scopus 로고
    • Copper coordination in the full-length, recombinant prion protein
    • Burns CS, et al. (2003) Copper coordination in the full-length, recombinant prion protein. Biochemistry 42:6794-6803.
    • (2003) Biochemistry , vol.42 , pp. 6794-6803
    • Burns, C.S.1
  • 19
    • 0034680507 scopus 로고    scopus 로고
    • Copper (II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study
    • Bonomo R, Impellizzeri G, Pappalardo G, Rizzarelli E, Tabbi G (2000) Copper (II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study. Chemistry 6:4195-4202.
    • (2000) Chemistry , vol.6 , pp. 4195-4202
    • Bonomo, R.1    Impellizzeri, G.2    Pappalardo, G.3    Rizzarelli, E.4    Tabbi, G.5
  • 20
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles J, et al. (1999) Copper binding to the prion protein: Structural implications of four identical cooperative binding sites. Proc Natl Acad Sci USA 96:2042-2047.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2042-2047
    • Viles, J.1
  • 21
    • 0035902531 scopus 로고    scopus 로고
    • Location and properties of metal-binding sites on the human prion protein
    • Jackson G, et al. (2001) Location and properties of metal-binding sites on the human prion protein. Proc Natl Acad Sci USA 98:8531-8535.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8531-8535
    • Jackson, G.1
  • 22
    • 13844299350 scopus 로고    scopus 로고
    • Probing copper(2+) binding to the prion protein-using diamagnetic nicke(2+) and H-1 NMR: The unstructured N terminus facilitates the coordination of six copper(2+) ions at physiological concentrations
    • Jones CE, Klewpatinond M, Abdelraheim SR, Brown DR, Viles JH (2005) Probing copper(2+) binding to the prion protein-using diamagnetic nicke(2+) and H-1 NMR: The unstructured N terminus facilitates the coordination of six copper(2+) ions at physiological concentrations. J Mol Biol 346:1393-1407.
    • (2005) J Mol Biol , vol.346 , pp. 1393-1407
    • Jones, C.E.1    Klewpatinond, M.2    Abdelraheim, S.R.3    Brown, D.R.4    Viles, J.H.5
  • 23
    • 38049006405 scopus 로고    scopus 로고
    • Hybrid ab initio Kohn-Sham density functional theory/frozen-density orbital-free density functional theory simulation method suitable for biological systems
    • Hodak M, Lu W, Bernholc J (2008) Hybrid ab initio Kohn-Sham density functional theory/frozen-density orbital-free density functional theory simulation method suitable for biological systems. J Chem Phys 128:014101.
    • (2008) J Chem Phys , vol.128 , pp. 014101
    • Hodak, M.1    Lu, W.2    Bernholc, J.3
  • 24
    • 0037254403 scopus 로고    scopus 로고
    • Computational studies of Cu(II)[peptide] binding motifs: Cu[hggg] and cu[hg] as models for Cu(II) binding to the prion protein octarepeat region
    • Pushie M, Rauk A (2003) Computational studies of Cu(II)[peptide] binding motifs: Cu[hggg] and cu[hg] as models for Cu(II) binding to the prion protein octarepeat region. J Biol Inorg Chem 8:53-65.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 53-65
    • Pushie, M.1    Rauk, A.2
  • 25
    • 24744456323 scopus 로고    scopus 로고
    • The octarepeat domain of the prion protein binds cu(II) with three distinct coordination modes at pH 7.4
    • Chattopadhyay M, et al. (2005) The octarepeat domain of the prion protein binds cu(II) with three distinct coordination modes at pH 7.4. J Am Chem Soc 127:12647-12656.
    • (2005) J Am Chem Soc , vol.127 , pp. 12647-12656
    • Chattopadhyay, M.1
  • 26
    • 33750534538 scopus 로고    scopus 로고
    • Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4
    • Wells M, et al. (2006) Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4. Biochem J 400:501-510.
    • (2006) Biochem J , vol.400 , pp. 501-510
    • Wells, M.1
  • 27
    • 33750571382 scopus 로고    scopus 로고
    • A reassessment of copper(II) binding in the full-length prion protein
    • Wells MA, et al. (2006) A reassessment of copper(II) binding in the full-length prion protein. Biochem J 399:435-444.
    • (2006) Biochem J , vol.399 , pp. 435-444
    • Wells, M.A.1
  • 28
    • 0034950034 scopus 로고    scopus 로고
    • Electron paramagnetic resonance evidence for binding of Cu2+ to the C-terminal domain of the murine prion protein
    • Cereghetti GM, et al. (2001) Electron paramagnetic resonance evidence for binding of Cu2+ to the C-terminal domain of the murine prion protein. Biophys J 81:516-525.
    • (2001) Biophys J , vol.81 , pp. 516-525
    • Cereghetti, G.M.1
  • 29
    • 0037343044 scopus 로고    scopus 로고
    • Stability and Cu (II) binding of prion protein variants related to inherited human prion diseases
    • Cereghetti GM, et al. (2003) Stability and Cu (II) binding of prion protein variants related to inherited human prion diseases. Biophys J 84:1985-1997.
    • (2003) Biophys J , vol.84 , pp. 1985-1997
    • Cereghetti, G.M.1
  • 30
    • 38549135029 scopus 로고    scopus 로고
    • Copper binding sites in the C-terminal domain of mouse prion protein: A hybrid (QM/MM) molecular dynamics study
    • Colombo MC, et al. (2008) Copper binding sites in the C-terminal domain of mouse prion protein: A hybrid (QM/MM) molecular dynamics study. Proteins 70:1084-1098.
    • (2008) Proteins , vol.70 , pp. 1084-1098
    • Colombo, M.C.1
  • 31
    • 1242316297 scopus 로고    scopus 로고
    • Copper binding in the prion protein
    • Millhauser G (2004) Copper binding in the prion protein. Acc Chem Res 37:79-85.
    • (2004) Acc Chem Res , vol.37 , pp. 79-85
    • Millhauser, G.1
  • 32
    • 1942518334 scopus 로고    scopus 로고
    • A theoretical study on Cu (II) binding modes and antioxidant activity of mammalian normal prion protein
    • Ji H, Zhang H (2004) A theoretical study on Cu (II) binding modes and antioxidant activity of mammalian normal prion protein. Chem Res Toxicol 17:471-475.
    • (2004) Chem Res Toxicol , vol.17 , pp. 471-475
    • Ji, H.1    Zhang, H.2
  • 33
    • 0033621029 scopus 로고    scopus 로고
    • Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence
    • Miura T, Hori-i A, Mototani H, Takeuchi H (1999) Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence. Biochemistry 38:11560-11569.
    • (1999) Biochemistry , vol.38 , pp. 11560-11569
    • Miura, T.1    Hori-i, A.2    Mototani, H.3    Takeuchi, H.4
  • 34
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • Millhauser G (2007) Copper and the prion protein: Methods, structures, function, and disease. Annu Rev Phys Chem 58:299-320.
    • (2007) Annu Rev Phys Chem , vol.58 , pp. 299-320
    • Millhauser, G.1
  • 35
    • 33751108289 scopus 로고    scopus 로고
    • The affinity of copper binding to the prion protein octarepeat domain: Evidence for negative cooperativity
    • Walter ED, Chattopadhyay M, Millhauser GL (2006) The affinity of copper binding to the prion protein octarepeat domain: Evidence for negative cooperativity. Biochemistry 45:13083-13092.
    • (2006) Biochemistry , vol.45 , pp. 13083-13092
    • Walter, E.D.1    Chattopadhyay, M.2    Millhauser, G.L.3
  • 36
    • 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. Chem Phys Lett 215:617-621.
    • (1993) Chem Phys Lett , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 37
    • 33749172039 scopus 로고    scopus 로고
    • CARMA: A molecular dynamics analysis program
    • Glykos NM (2006) CARMA: A molecular dynamics analysis program. J Comput Chem 27:1765-1768.
    • (2006) J Comput Chem , vol.27 , pp. 1765-1768
    • Glykos, N.M.1
  • 38
    • 0005309671 scopus 로고
    • Extracellular copper substituents and mammalian copper transport
    • Plenum, New York, pp
    • Linder M (1991) Extracellular copper substituents and mammalian copper transport. Biochemistry of Copper (Plenum, New York), pp 73-134.
    • (1991) Biochemistry of Copper , pp. 73-134
    • Linder, M.1
  • 39
    • 0027520019 scopus 로고
    • Intrinsic stoichiometric equilibrium constants for the binding of zinc (II) and copper (II) to the high affinity site of serum albumin
    • Masuoka J, Hegenauer J, Van Dyke B, Saltman P (1993) Intrinsic stoichiometric equilibrium constants for the binding of zinc (II) and copper (II) to the high affinity site of serum albumin. J Biol Chem 268:21533-21537.
    • (1993) J Biol Chem , vol.268 , pp. 21533-21537
    • Masuoka, J.1    Hegenauer, J.2    Van Dyke, B.3    Saltman, P.4
  • 40
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, Argos P (1995) Knowledge-based protein secondary structure assignment. Proteins Struct Funct Genet 23:566-579.
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 41
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 42
    • 18344391235 scopus 로고    scopus 로고
    • Copper (II) inhibits in vitro conversion of prion protein into amyloid fibrils
    • Bocharova O, Breydo L, Salnikov V, Baskakov I (2005) Copper (II) inhibits in vitro conversion of prion protein into amyloid fibrils. Biochemistry 44:6776-6787.
    • (2005) Biochemistry , vol.44 , pp. 6776-6787
    • Bocharova, O.1    Breydo, L.2    Salnikov, V.3    Baskakov, I.4
  • 44
    • 0033130083 scopus 로고    scopus 로고
    • Strain-specific prion-protein conformation determined by metal ions
    • Wadsworth J, et al. (1999) Strain-specific prion-protein conformation determined by metal ions. Nat Cell Biol 1:55-59.
    • (1999) Nat Cell Biol , vol.1 , pp. 55-59
    • Wadsworth, J.1
  • 45
    • 0345306739 scopus 로고    scopus 로고
    • Copper chelation delays the onset of prion disease*
    • Sigurdsson E, et al. (2003) Copper chelation delays the onset of prion disease*. J Biol Chem 278:46199-46202.
    • (2003) J Biol Chem , vol.278 , pp. 46199-46202
    • Sigurdsson, E.1
  • 46
    • 0034705438 scopus 로고    scopus 로고
    • Copper (II)-induced conformational changes and protease resistance in recombinant and cellular PrP effect of protein age and deamidation
    • Qin K, et al. (2000) Copper (II)-induced conformational changes and protease resistance in recombinant and cellular PrP effect of protein age and deamidation. J Biol Chem 275:19121-19131.
    • (2000) J Biol Chem , vol.275 , pp. 19121-19131
    • Qin, K.1
  • 47
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions-Dielectric, electrostatic and steric stabilization of carbonium-ion in reaction of lysozyme
    • Warshel A, Levitt M (1976) Theoretical studies of enzymic reactions-Dielectric, electrostatic and steric stabilization of carbonium-ion in reaction of lysozyme. J Mol Biol 102:227-249.
    • (1976) J Mol Biol , vol.102 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 48
    • 84988053595 scopus 로고
    • A combined ab initio quantum-mechanical and molecular mechanical method for carrying out simulations on complex molecular-systems - Applications to the ch3cl + cl- exchange-reaction and gas-phase protonation of polyethers
    • Singh UC, Kollmann PA (1986) A combined ab initio quantum-mechanical and molecular mechanical method for carrying out simulations on complex molecular-systems - Applications to the ch3cl + cl- exchange-reaction and gas-phase protonation of polyethers. J Comput Chem 7:718-730.
    • (1986) J Comput Chem , vol.7 , pp. 718-730
    • Singh, U.C.1    Kollmann, P.A.2
  • 49
    • 84986513644 scopus 로고
    • A combined quantum-mechanical and molecular mechanical potential for molecular-dynamics simulations
    • Field MJ, Bash PA, Karplus M (1990) A combined quantum-mechanical and molecular mechanical potential for molecular-dynamics simulations. J Comput Chem 11:700-733.
    • (1990) J Comput Chem , vol.11 , pp. 700-733
    • Field, M.J.1    Bash, P.A.2    Karplus, M.3
  • 50
    • 0000054413 scopus 로고    scopus 로고
    • Real-space multigrid-based approach to large-scale electronic structure calculations
    • Briggs EL, Sullivan DJ, Bernholc J (1996) Real-space multigrid-based approach to large-scale electronic structure calculations. Phys Rev B 54:14362-14375.
    • (1996) Phys Rev B , vol.54 , pp. 14362-14375
    • Briggs, E.L.1    Sullivan, D.J.2    Bernholc, J.3
  • 51
    • 34547673564 scopus 로고    scopus 로고
    • Implementation of ultrasoft pseudopotentials in large-scale grid-based electronic structure calculations
    • Hodak M, Wang S, Lu W, Bernholc J (2007) Implementation of ultrasoft pseudopotentials in large-scale grid-based electronic structure calculations. Phys Rev B 76:085108.
    • (2007) Phys Rev B , vol.76 , pp. 085108
    • Hodak, M.1    Wang, S.2    Lu, W.3    Bernholc, J.4
  • 52
    • 20544463457 scopus 로고
    • Soft self-consistent pseudopotentials in a generalized eigenvalue formalism
    • Vanderbilt D (1990) Soft self-consistent pseudopotentials in a generalized eigenvalue formalism. Phys Rev B 41:7892.
    • (1990) Phys Rev B , vol.41 , pp. 7892
    • Vanderbilt, D.1
  • 53
    • 4243943295 scopus 로고    scopus 로고
    • Generalized gradient approximation made simple
    • Perdew JP, Burke K, Ernzerhof M (1996) Generalized gradient approximation made simple. Phys Rev Lett 77:3865.
    • (1996) Phys Rev Lett , vol.77 , pp. 3865
    • Perdew, J.P.1    Burke, K.2    Ernzerhof, M.3
  • 55
    • 0012710491 scopus 로고    scopus 로고
    • NMRsolution structure of the human prion protein
    • Zahn R, et al. (2000)NMRsolution structure of the human prion protein. Proc Natl Acad Sci USA 97:145-150.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 145-150
    • Zahn, R.1
  • 56
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with namd
    • Phillips JC, et al. (2005) Scalable molecular dynamics with namd. J Comput Chem 26:1781-1802.
    • (2005) J Comput Chem , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 57
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller SE, MacKerell AD (2000) An improved empirical potential energy function for molecular simulations of phospholipids. J Phys Chem B 104:7510-7515.
    • (2000) J Phys Chem B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, A.D.2
  • 58
    • 0028867364 scopus 로고
    • Constant pressure and temperature molecular dynamics simulation of a fully hydrated liquid crystal phase dipalmitoylphosphatidylcholine bilayer
    • Tu K, Tobias DJ, Klein ML (1995) Constant pressure and temperature molecular dynamics simulation of a fully hydrated liquid crystal phase dipalmitoylphosphatidylcholine bilayer. Biophys J 69:2558-2562.
    • (1995) Biophys J , vol.69 , pp. 2558-2562
    • Tu, K.1    Tobias, D.J.2    Klein, M.L.3
  • 59
    • 36449007836 scopus 로고
    • Constant-pressure moleculardynamics simulation-The Langevin piston method
    • Feller SE, Zhang YH, Pastor RW, Brooks BR (1995) Constant-pressure moleculardynamics simulation-The Langevin piston method. J Chem Phys 103:4613-4621.
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 60
    • 33646650705 scopus 로고
    • Reversible multiple time scale moleculardynamics
    • Tuckerman M, Berne BJ, Martyna GJ (1992) Reversible multiple time scale moleculardynamics. J Chem Phys 97:1990-2001.
    • (1992) J Chem Phys , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.J.2    Martyna, G.J.3
  • 61
    • 84963146276 scopus 로고
    • Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions
    • Grubmüller H, Heller H, Windemuth A, Schulten K (1991) Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions. Mol Simul 6:121-142.
    • (1991) Mol Simul , vol.6 , pp. 121-142
    • Grubmüller, H.1    Heller, H.2    Windemuth, A.3    Schulten, K.4
  • 62
    • 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 (1977) Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes. J Comput Phys 23:327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.