메뉴 건너뛰기




Volumn 33, Issue 14, 2007, Pages 1143-1154

Molecular dynamics simulation of human interleukin-4: Comparison with NMR data and effect of pH, counterions and force field on tertiary structure stability

Author keywords

Counterions; Interleukin 4; Low pH; Molecular dynamics simulation; Unfolding

Indexed keywords

COMPUTER SIMULATION; NUCLEAR MAGNETIC RESONANCE; PARAMETER ESTIMATION; PROTEINS; PROTONS; SOLUTIONS;

EID: 36949031938     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927020701613623     Document Type: Article
Times cited : (2)

References (77)
  • 1
    • 0035910479 scopus 로고    scopus 로고
    • The key to solving the protein-folding problem lies in an accurate description of the denatured state
    • W.F. van Gunsteren, R. Bürgi, C. Peter, X. Daura. The key to solving the protein-folding problem lies in an accurate description of the denatured state. Angew. Chem. Int. Ed, Eng., 40, 351 (2001).
    • (2001) Angew. Chem. Int. Ed, Eng , vol.40 , pp. 351
    • van Gunsteren, W.F.1    Bürgi, R.2    Peter, C.3    Daura, X.4
  • 2
    • 0035905573 scopus 로고    scopus 로고
    • A.R. Dinner, M. Karplus. Comment on the communication. The key to solving the protein-folding problem lies in an accurate description of the denatured state by van Gunsteren et al. Angew. Chem, Int. Ed. Eng., 40, 4615 (2001).
    • A.R. Dinner, M. Karplus. Comment on the communication. The key to solving the protein-folding problem lies in an accurate description of the denatured state by van Gunsteren et al. Angew. Chem, Int. Ed. Eng., 40, 4615 (2001).
  • 3
    • 36949019010 scopus 로고    scopus 로고
    • W.F. van Gunsteren, R. Bürgi, C Peter, X. Daura. Reply to the comment on the communication by van Gunsteren et al. Angew. Chem, Int. Ed. Eng., 40, 351 (2001)
    • W.F. van Gunsteren, R. Bürgi, C Peter, X. Daura. Reply to the comment on the communication by van Gunsteren et al. Angew. Chem, Int. Ed. Eng., 40, 351 (2001)
  • 4
    • 0035905564 scopus 로고    scopus 로고
    • Angew. Chem, Int. Ed., 40, 4616-4618, 2001.
    • (2001) Chem, Int. Ed , vol.40 , pp. 4616-4618
    • Angew1
  • 5
    • 0014364651 scopus 로고
    • Protein denaturation
    • C Tanford. Protein denaturation. Adv. Protein Chem., 23, 121 (1968).
    • (1968) Adv. Protein Chem , vol.23 , pp. 121
    • Tanford, C.1
  • 6
  • 7
    • 0001931668 scopus 로고
    • Unfolded proteins, compact states and molten globules
    • CM. Dobson. Unfolded proteins, compact states and molten globules. Curr. Opin, Struct. Biol., 2, 6 (1992).
    • (1992) Curr. Opin, Struct. Biol , vol.2 , pp. 6
    • Dobson, C.M.1
  • 8
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • CM. Dobson. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol., 15, 3 (2004).
    • (2004) Semin. Cell Dev. Biol , vol.15 , pp. 3
    • Dobson, C.M.1
  • 9
    • 0028466243 scopus 로고
    • Protein-folding-solid evidence for molten globules
    • C.M. Dobson. Protein-folding-solid evidence for molten globules. Curr. Biol., 4, 636 (1994).
    • (1994) Curr. Biol , vol.4 , pp. 636
    • Dobson, C.M.1
  • 10
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • M. Arai, K. Kuwajima. Role of the molten globule state in protein folding. Adv. Protein Chem., 53, 209 (2000).
    • (2000) Adv. Protein Chem , vol.53 , pp. 209
    • Arai, M.1    Kuwajima, K.2
  • 11
    • 0025764757 scopus 로고
    • Interleukin-4: A prototypic immunoregulatory lymphokine
    • W.E. Paul. Interleukin-4: a prototypic immunoregulatory lymphokine. Blood, 77, 1859(1991).
    • (1991) Blood , vol.77 , pp. 1859
    • Paul, W.E.1
  • 13
    • 0028201726 scopus 로고
    • Acquisition of lymphokine-producing phenotype by CD4 + T-cells
    • R.A. Seder, WE. Paul. Acquisition of lymphokine-producing phenotype by CD4 + T-cells. Annu. Rev, Immunol., 12, 635 (1994).
    • (1994) Annu. Rev, Immunol , vol.12 , pp. 635
    • Seder, R.A.1    Paul, W.E.2
  • 14
    • 0034683059 scopus 로고    scopus 로고
    • The interleukin-4-receptor: From recognition mechanism to pharmacological target structure
    • P. Reinemer, W. Sebald, A. Duschl. The interleukin-4-receptor: from recognition mechanism to pharmacological target structure. Angew. Chem. Int. Ed, Eng., 39, 2834 (2000).
    • (2000) Angew. Chem. Int. Ed, Eng , vol.39 , pp. 2834
    • Reinemer, P.1    Sebald, W.2    Duschl, A.3
  • 16
    • 0026764439 scopus 로고
    • 3-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magneticresonance spectroscopy
    • R. Powers, D.S. Garrett, C.J. Marchand, E.A. Frieden, A.M. Gronenborn, G.M. Clore. 3-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magneticresonance spectroscopy. Science, 256, 1673 (1992).
    • (1992) Science , vol.256 , pp. 1673
    • Powers, R.1    Garrett, D.S.2    Marchand, C.J.3    Frieden, E.A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 17
    • 0026661731 scopus 로고
    • Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution
    • A. Wlodawer, A. Pavlovsky, A. Gustchina. Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution. FEBS Lett., 309, 59 (1992).
    • (1992) FEBS Lett , vol.309 , pp. 59
    • Wlodawer, A.1    Pavlovsky, A.2    Gustchina, A.3
  • 19
    • 0028914794 scopus 로고
    • Human interleukin-4 and variant R88Q: Phasing X-ray diffraction data by molecular replacement using X-ray and nuclear-magnetic-resonance models
    • T. Müller, F. Oehlenschlager, M. Buehner. Human interleukin-4 and variant R88Q: phasing X-ray diffraction data by molecular replacement using X-ray and nuclear-magnetic-resonance models. J, Mol. Biol., 247, 360 (1995).
    • (1995) J, Mol. Biol , vol.247 , pp. 360
    • Müller, T.1    Oehlenschlager, F.2    Buehner, M.3
  • 20
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor super-family
    • J.F. Bazan. Structural design and molecular evolution of a cytokine receptor super-family. Proc Natl. Acad, Sci. USA, 87, 6934 (1990).
    • (1990) Proc Natl. Acad, Sci. USA , vol.87 , pp. 6934
    • Bazan, J.F.1
  • 22
    • 0026478643 scopus 로고
    • Loop mobility in a four-helix-bundle protein: N NMR relaxation measurements on human interleukin-4
    • C Redfield, J. Boyd, L.J. Smith, R.A.G. Smith, CM. Dobson. Loop mobility in a four-helix-bundle protein: N NMR relaxation measurements on human interleukin-4. Biochemistry, 31, 10431 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10431
    • Redfield, C.1    Boyd, J.2    Smith, L.J.3    Smith, R.A.G.4    Dobson, C.M.5
  • 23
    • 0028367331 scopus 로고
    • Structural, characterization of a highly-ordered molten globule at low pH
    • C. Redfield, R.A.G. Smith, C.M. Dobson. Structural, characterization of a highly-ordered molten globule at low pH. Nat. Struct. Biol., 1, 23 (1994).
    • (1994) Nat. Struct. Biol , vol.1 , pp. 23
    • Redfield, C.1    Smith, R.A.G.2    Dobson, C.M.3
  • 24
    • 0026630480 scopus 로고
    • Simulation of the thermal denaturation of hen egg-white lysozyme-trapping the molten globule state
    • A.E. Mark, W.F. van Gunsteren. Simulation of the thermal denaturation of hen egg-white lysozyme-trapping the molten globule state. Biochemistry, 31, 7745 (1992).
    • (1992) Biochemistry , vol.31 , pp. 7745
    • Mark, A.E.1    van Gunsteren, W.F.2
  • 25
    • 0026694167 scopus 로고
    • A model of the molten globule state from molecular-dynamics simulations
    • V Dagget, M. Levitt. A model of the molten globule state from molecular-dynamics simulations. Proc. Natl. Acad. Sci. USA, 89, 5142(1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5142
    • Dagget, V.1    Levitt, M.2
  • 26
    • 0033168453 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human a-lactalbumin: Changes to the structural and dynamical properties of the protein at low pH
    • L.J. Smith, C.M. Dobson, W.F. van Gunsteren. Molecular dynamics simulations of human a-lactalbumin: changes to the structural and dynamical properties of the protein at low pH. Proteins, 36, 77 (1999).
    • (1999) Proteins , vol.36 , pp. 77
    • Smith, L.J.1    Dobson, C.M.2    van Gunsteren, W.F.3
  • 27
    • 0033548540 scopus 로고    scopus 로고
    • Side-chain conformational disorder in a molten globule: Molecular dynamics simulations of the A-state of human a-lactalbumin
    • L.J. Smith, C.M. Dobson, W.F. van Gunsteren. Side-chain conformational disorder in a molten globule: molecular dynamics simulations of the A-state of human a-lactalbumin. J. Mol Biol., 286, 1567 (1999).
    • (1999) J. Mol Biol , vol.286 , pp. 1567
    • Smith, L.J.1    Dobson, C.M.2    van Gunsteren, W.F.3
  • 28
    • 0041819710 scopus 로고    scopus 로고
    • Relative stability of protein structures determined by X-ray crystallography or NMR-spectroscopy: A molecular dynamics simulation study
    • H. Fan, A.E. Mark. Relative stability of protein structures determined by X-ray crystallography or NMR-spectroscopy: a molecular dynamics simulation study. Proteins, 53, 111 (2003).
    • (2003) Proteins , vol.53 , pp. 111
    • Fan, H.1    Mark, A.E.2
  • 29
    • 0031834850 scopus 로고    scopus 로고
    • Importance of explicit salt ions for protein stability in molecular dynamics simulation
    • G.T. Ibragimova, R.C. Wade. Importance of explicit salt ions for protein stability in molecular dynamics simulation. Biophys. J, 74, 2906 (1998).
    • (1998) Biophys. J , vol.74 , pp. 2906
    • Ibragimova, G.T.1    Wade, R.C.2
  • 30
    • 0031763268 scopus 로고    scopus 로고
    • Effects of counter-ions and volume on the simulated dynamics of solvated proteins. Application to the activation domain of procarboxypeptidase B
    • M.A. Marti-Renom, J.M. Mas, B. Oliva, E. Querol, F.X. Aviles. Effects of counter-ions and volume on the simulated dynamics of solvated proteins. Application to the activation domain of procarboxypeptidase B. Protein Eng., 11, 881 (1998).
    • (1998) Protein Eng , vol.11 , pp. 881
    • Marti-Renom, M.A.1    Mas, J.M.2    Oliva, B.3    Querol, E.4    Aviles, F.X.5
  • 31
    • 0033135037 scopus 로고    scopus 로고
    • + ions on simulated structure and dynamics of beta ARK1. PH domain. Proteins Struct. Funct. Genet., 35, 206 (1999).
    • + ions on simulated structure and dynamics of beta ARK1. PH domain. Proteins Struct. Funct. Genet., 35, 206 (1999).
  • 32
    • 0035664220 scopus 로고    scopus 로고
    • The investigation of the effects of counterions in protein dynamics simulations
    • P. Drabik, A. Liwo, C Czaplewski, J. Ciarkowski, The investigation of the effects of counterions in protein dynamics simulations. Protein Eng., 14, 747 (2001).
    • (2001) Protein Eng , vol.14 , pp. 747
    • Drabik, P.1    Liwo, A.2    Czaplewski, C.3    Ciarkowski, J.4
  • 33
    • 84986518863 scopus 로고
    • AMBER: Assisted model building with energy refinement. A general program for modeling molecules and their interactions
    • P.K. Weiner, P.A. Kollman. AMBER: assisted model building with energy refinement. A general program for modeling molecules and their interactions. J. Comput. Chem., 2, 287 (1981).
    • (1981) J. Comput. Chem , vol.2 , pp. 287
    • Weiner, P.K.1    Kollman, P.A.2
  • 35
    • 0029633186 scopus 로고    scopus 로고
    • D.A. Pearlman, D.A. Case, J.W. Caldwell, W.S. Ross, TE. Cheatham III, S. DeBolt, D. Ferguson, G. Seibel, P.A. Kollman. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun., 91, 1 (1995).
    • D.A. Pearlman, D.A. Case, J.W. Caldwell, W.S. Ross, TE. Cheatham III, S. DeBolt, D. Ferguson, G. Seibel, P.A. Kollman. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun., 91, 1 (1995).
  • 37
    • 6344260593 scopus 로고
    • An all-atom, empirical energy function for the simulation of nucleic acids
    • A.D. MacKerell Jr., J. Wirkiewicz-Kuczera, M. Karplus. An all-atom, empirical energy function for the simulation of nucleic acids. J. Am. Chem. Soc., 117, 11946 (1975).
    • (1975) J. Am. Chem. Soc , vol.117 , pp. 11946
    • MacKerell Jr., A.D.1    Wirkiewicz-Kuczera, J.2    Karplus, M.3
  • 39
    • 33645941402 scopus 로고    scopus 로고
    • W.L. Jorgensen, J. Tirado-Rives. The OPLS potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc., 110, 1657 (1988).
    • W.L. Jorgensen, J. Tirado-Rives. The OPLS potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc., 110, 1657 (1988).
  • 40
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformationalenergetics and properties of organic liquids
    • W.L. Jorgensen, D.S. Maxwell, J. Tirado-Rives. Development and testing of the OPLS all-atom force field on conformationalenergetics and properties of organic liquids. J. Am. Chem. Soc., 118, 11225(1996).
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11225
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 43
    • 0035425883 scopus 로고    scopus 로고
    • An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase
    • L..D, Schuler, X. Daura, W.F. van Gunsteren. An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase. J. Comput. Chem., 22, 1205 (2001).
    • (2001) J. Comput. Chem , vol.22 , pp. 1205
    • Schuler, L.D.1    Daura, X.2    van Gunsteren, W.F.3
  • 44
    • 0037089015 scopus 로고    scopus 로고
    • Calculation of the free energy of solvation for neutral analogs of amino acid side chains
    • A. Villa, A.E. Mark. Calculation of the free energy of solvation for neutral analogs of amino acid side chains. J. Comput. Chem., 23, 548 (2002).
    • (2002) J. Comput. Chem , vol.23 , pp. 548
    • Villa, A.1    Mark, A.E.2
  • 45
    • 0142250484 scopus 로고    scopus 로고
    • Calculation of the watercyclohexane transfer free energies of neutral amino acid sidechain analogs using the OPLS all-atom force field
    • J.L. MacCallum, D.P. Tieleman. Calculation of the watercyclohexane transfer free energies of neutral amino acid sidechain analogs using the OPLS all-atom force field. J. Comput. Chem., 24, 1930(2003).
    • (2003) J. Comput. Chem , vol.24 , pp. 1930
    • MacCallum, J.L.1    Tieleman, D.P.2
  • 46
    • 0141990949 scopus 로고    scopus 로고
    • Extremely precise free energy calculations of amino acid side chain analogs: Comparison of common molecular mechanics force fields for proteins
    • M.R. Shirts, J.W. Pitera, W.C. Swope, V.S. Pande. Extremely precise free energy calculations of amino acid side chain analogs: comparison of common molecular mechanics force fields for proteins. J. Chem. Phys., 119, 5740 (2003).
    • (2003) J. Chem. Phys , vol.119 , pp. 5740
    • Shirts, M.R.1    Pitera, J.W.2    Swope, W.C.3    Pande, V.S.4
  • 47
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • C. Oostenbrink, A. Villa, A.E. Mark, W.F. van Gunsteren. A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem., 25, 1656 (2004).
    • (2004) J. Comput. Chem , vol.25 , pp. 1656
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    van Gunsteren, W.F.4
  • 49
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • B. Pullman Ed, pp, Reidel, Dordrecht
    • H.J.C. Berendsen, J.P.M, Postma, W.F. van Gunsteren, J. Hermans. Interaction models for water in relation to protein hydration. In Intermolecular Forces, B. Pullman (Ed.), pp. 331-342, Reidel, Dordrecht (1981).
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    van Gunsteren, W.F.3    Hermans, J.4
  • 50
    • 33646940952 scopus 로고
    • Numerical, integration of the cartesian equations of motion of a system, with constraints: Molecular dynamics of n-alkanes
    • J.R Ryckaert, G. Ciccotti, H.J.C. Berendsen. Numerical, integration of the cartesian equations of motion of a system, with constraints: molecular dynamics of n-alkanes. J. Comput. Phys., 23, 327 (1977).
    • (1977) J. Comput. Phys , vol.23 , pp. 327
    • Ryckaert, J.R.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 51
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular dynamics simulations
    • I.G. Tironi, R. Sperb, P.E. Smith, W.F. van Gunsteren. A generalized reaction field method for molecular dynamics simulations. J. Chem. Phys., 102, 5451 (1995).
    • (1995) J. Chem. Phys , vol.102 , pp. 5451
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    van Gunsteren, W.F.4
  • 52
    • 0037042610 scopus 로고    scopus 로고
    • Derivation of an improved simple point charge model for liquid water: SPC/A and SPC/L
    • A. Glättli, X. Daura, W.F. van Gunsteren. Derivation of an improved simple point charge model for liquid water: SPC/A and SPC/L. J. Chem. Phys., 116, 9811 (2002).
    • (2002) J. Chem. Phys , vol.116 , pp. 9811
    • Glättli, A.1    Daura, X.2    van Gunsteren, W.F.3
  • 54
    • 0001490366 scopus 로고    scopus 로고
    • Calculating electrostatic interactions using the parti cle-particle particle-mesh method with nonperiodic long-range interactions
    • B.A. Luty, W.F. van Gunsteren. Calculating electrostatic interactions using the parti cle-particle particle-mesh method with nonperiodic long-range interactions. J. Phys. Chem., 100, 2581 (1996).
    • (1996) J. Phys. Chem , vol.100 , pp. 2581
    • Luty, B.A.1    van Gunsteren, W.F.2
  • 55
    • 0001465838 scopus 로고    scopus 로고
    • Space-time correlated reaction field: A stochastic dynamical approach to the dielectric continuum
    • I.G. Tironi, B.A, Luty, W.F. van Gunsteren. Space-time correlated reaction field: a stochastic dynamical approach to the dielectric continuum. J. Chem. Phys., 106, 6068 (1997).
    • (1997) J. Chem. Phys , vol.106 , pp. 6068
    • Tironi, I.G.1    Luty, B.A.2    van Gunsteren, W.F.3
  • 56
    • 0038683517 scopus 로고    scopus 로고
    • Ewald artifacts in computer simulations of ionic solvation and ion-ion interaction: A continuum, electrostatics study
    • P.H. Hünenberger, J.A. McCammon. Ewald artifacts in computer simulations of ionic solvation and ion-ion interaction: a continuum, electrostatics study. J. Chem. Phys., 110, 1856 (1999).
    • (1999) J. Chem. Phys , vol.110 , pp. 1856
    • Hünenberger, P.H.1    McCammon, J.A.2
  • 57
    • 0037627173 scopus 로고    scopus 로고
    • Effect of artificial periodicity in simulations of biomolecules under Ewald boundary conditions: A continuum electrostatics study
    • P.H. Hünenberger, J.A. McCammon. Effect of artificial periodicity in simulations of biomolecules under Ewald boundary conditions: a continuum electrostatics study. Biophys, Chem., 78, 69 (1999).
    • (1999) Biophys, Chem , vol.78 , pp. 69
    • Hünenberger, P.H.1    McCammon, J.A.2
  • 58
    • 0343005873 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a polyalanine octapeptide under Ewald boundary conditions: Influence of artificial periodicity on peptide conformation
    • W. Weber, P.H. Hünenberger, J.A. McCammon. Molecular dynamics simulations of a polyalanine octapeptide under Ewald boundary conditions: influence of artificial periodicity on peptide conformation. J. Phys. Chem. B, 104, 3668 (2000).
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3668
    • Weber, W.1    Hünenberger, P.H.2    McCammon, J.A.3
  • 59
    • 0001735019 scopus 로고    scopus 로고
    • Ewald summation and reactions field methods for potentials with atomic charges, dipoles, and polarizabilities
    • TM. Nymand, P. Linse. Ewald summation and reactions field methods for potentials with atomic charges, dipoles, and polarizabilities. J. Chem. Phys., 112, 6152 (2000).
    • (2000) J. Chem. Phys , vol.112 , pp. 6152
    • Nymand, T.M.1    Linse, P.2
  • 60
    • 17144471008 scopus 로고    scopus 로고
    • Comparison of different schemes to treat long-range electrostatic interactions in molecular dynamics simulations of a protein crystal
    • R. Walser, P.H. Hünenberger, W.F. van Gunsteren. Comparison of different schemes to treat long-range electrostatic interactions in molecular dynamics simulations of a protein crystal. Proteins, 43, 509 (2001).
    • (2001) Proteins , vol.43 , pp. 509
    • Walser, R.1    Hünenberger, P.H.2    van Gunsteren, W.F.3
  • 62
    • 36949020935 scopus 로고    scopus 로고
    • W.F. van Gunsteren, R. Boelens, R. Kaptein, R.M. Scheek, E.R.P. Zuiderweg. An Improved Restrained Molecular Dynamics Technique to Obtain Protein Tertiary Structure from Nuclear Magnetic Data. Polycrystal Book Service, P. O. Box 27, 60558 Western Springs, ILL (1985).
    • W.F. van Gunsteren, R. Boelens, R. Kaptein, R.M. Scheek, E.R.P. Zuiderweg. An Improved Restrained Molecular Dynamics Technique to Obtain Protein Tertiary Structure from Nuclear Magnetic Data. Polycrystal Book Service, P. O. Box 27, 60558 Western Springs, ILL (1985).
  • 63
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common am.ino-aci.ds for use in studies of protein conformations by measurements of intramolecular proton proton distance constraints with, nuclear magnetic-resonance
    • K. Wüthrich, M. Billeter, W. Braun. Pseudo-structures for the 20 common am.ino-aci.ds for use in studies of protein conformations by measurements of intramolecular proton proton distance constraints with, nuclear magnetic-resonance. J. Mol. Biol., 169, 949 (1983).
    • (1983) J. Mol. Biol , vol.169 , pp. 949
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 66
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structurepattern- recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, C Sander. Dictionary of protein secondary structurepattern- recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577 (1983).
    • (1983) Biopolymers , vol.22 , pp. 2577
    • Kabsch, W.1    Sander, C.2
  • 67
    • 36749110658 scopus 로고
    • Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: The effect of fluctuating intemuclear distances
    • J. Tropp. Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: the effect of fluctuating intemuclear distances. J. Chem. Phys., 72, 6035 (1980).
    • (1980) J. Chem. Phys , vol.72 , pp. 6035
    • Tropp, J.1
  • 68
    • 33745356391 scopus 로고
    • Contact electron-spin coupling of nuclear magnetic moments
    • M. Karplus. Contact electron-spin coupling of nuclear magnetic moments. J. Chem. Phys., 30, 11 (1959).
    • (1959) J. Chem. Phys , vol.30 , pp. 11
    • Karplus, M.1
  • 69
    • 12044259775 scopus 로고    scopus 로고
    • 15N-enriched proteins. J. Am. Chem. Soc., 115, 7772 (1993).
    • 15N-enriched proteins. J. Am. Chem. Soc., 115, 7772 (1993).
  • 70
    • 0000279972 scopus 로고
    • Influence of vibrational motion on solid-state line-shapes and NMR relaxation
    • E.R. Henry, A. Szabo. Influence of vibrational motion on solid-state line-shapes and NMR relaxation. J. Chem. Phys., 82, 4753 (1985).
    • (1985) J. Chem. Phys , vol.82 , pp. 4753
    • Henry, E.R.1    Szabo, A.2
  • 72
    • 0033546403 scopus 로고    scopus 로고
    • Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations
    • J. Evenäs, S. Forsén, A. Malmendal, M. Akke. Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations. J. Mol. Biol., 289, 603 (1999).
    • (1999) J. Mol. Biol , vol.289 , pp. 603
    • Evenäs, J.1    Forsén, S.2    Malmendal, A.3    Akke, M.4
  • 73
    • 0033783932 scopus 로고    scopus 로고
    • On the similarity of properties in solution or in the crystalline state: A molecular dynamics study of hen lysozyme
    • U. Stocker, K. Spiegel, W.F. van Gunsteren. On the similarity of properties in solution or in the crystalline state: a molecular dynamics study of hen lysozyme. J. Biomol. NMR, 18, 1 (2000).
    • (2000) J. Biomol. NMR , vol.18 , pp. 1
    • Stocker, U.1    Spiegel, K.2    van Gunsteren, W.F.3
  • 74
    • 3042616027 scopus 로고    scopus 로고
    • Effect of methylation on the stability and solvation free energy of amylose and cellulose fragments: A molecular dynamics study
    • H.B. Yu, M. Amann, T. Hansson, J. Köhler, G. Wich, W.F. van Gunsteren. Effect of methylation on the stability and solvation free energy of amylose and cellulose fragments: a molecular dynamics study. Carbohydr. Res., 339, 1697 (2004).
    • (2004) Carbohydr. Res , vol.339 , pp. 1697
    • Yu, H.B.1    Amann, M.2    Hansson, T.3    Köhler, J.4    Wich, G.5    van Gunsteren, W.F.6
  • 75
    • 11244289541 scopus 로고    scopus 로고
    • Validation of the GROMOS force-field parameter set 45A3 against nuclear magnetic resonance data of hen egg lysozyme
    • T. Soares, X. Daura, C Oostenbrink, L.J. Smith, W.F. van Gunsteren. Validation of the GROMOS force-field parameter set 45A3 against nuclear magnetic resonance data of hen egg lysozyme. J. Biomol. NMR, 30, 407 (2004).
    • (2004) J. Biomol. NMR , vol.30 , pp. 407
    • Soares, T.1    Daura, X.2    Oostenbrink, C.3    Smith, L.J.4    van Gunsteren, W.F.5
  • 76
  • 77
    • 0038420254 scopus 로고    scopus 로고
    • Ionic conductivity and diffusion at infinite dilution
    • 79th ed, p, CRC, Boca Raton, FL
    • P. Vanysek. Ionic conductivity and diffusion at infinite dilution. CRC Handbook of Chemistry and Physics, 79th ed., p. 86, CRC, Boca Raton, FL (2006).
    • (2006) CRC Handbook of Chemistry and Physics , pp. 86
    • Vanysek, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.