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Volumn 24, Issue 3, 1991, Pages 227-291

Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; GLOBULAR PROTEIN; HEMOPROTEIN; HEXOKINASE; LIGAND; MYOGLOBIN; PROTEIN; WATER;

EID: 0025938315     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583500003723     Document Type: Article
Times cited : (312)

References (182)
  • 1
    • 0038336106 scopus 로고
    • Quasiclassical treatment of neutron scattering
    • 1165–1167
    • Aamodt, R., Case, K. M., Rosenbaum, M. & Zweiful, P. F. (1962). Quasiclassical treatment of neutron scattering. Phys. Rev. 126 (3), 1165–1167.
    • (1962) Phys. Rev , vol.126 , Issue.3
    • Aamodt, R.1    Case, K.M.2    Rosenbaum, M.3    Zweiful, P.F.4
  • 2
    • 0001175209 scopus 로고
    • Computer simulation of ionic systems: the distorting effects of the boundary conditions
    • 329–332
    • Adams, D. (1979). Computer simulation of ionic systems: the distorting effects of the boundary conditions. Chem. Phys. Lett. 62, 329–332.
    • (1979) Chem. Phys. Lett. 62
    • Adams, D.1
  • 3
    • 36749119688 scopus 로고
    • CO binding to heme proteins: A model for barrier height distributions and slow conformational changes
    • 2042–2053
    • Agmon, N. & Hopfield, J. J. (1983). CO binding to heme proteins: A model for barrier height distributions and slow conformational changes. J. chem. Phys. 79 (4), 2042–2053
    • (1983) J. chem. Phys , vol.79 , Issue.4
    • Agmon, N.1    Hopfield, J.J.2
  • 5
    • 33845281367 scopus 로고
    • Molecular dynamics simulation of parvalbumin in aqueous solution
    • Ahlstrom, P., Teleman, O., Jonsson, B. & Forsen, S. (1987). Molecular dynamics simulation of parvalbumin in aqueous solution. J. Am. chem. Soc. 109, 1541–1551.
    • (1987) J. Am. chem. Soc , vol.109 , pp. 1541-1551
    • Ahlstrom, P.1    Teleman, O.2    Jonsson, B.3    Forsen, S.4
  • 6
    • 0023357309 scopus 로고
    • Interpretation of fluoresence decays in proteins using continuous lifetime distributions
    • 925–936
    • Alcala, J. R., Gratton, E. & Prendergast, F. G. (1987). Interpretation of fluoresence decays in proteins using continuous lifetime distributions. Biophys. J. 51, 925–936.
    • (1987) Biophys. J , vol.51
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 7
    • 0020186194 scopus 로고
    • Density of states on fractals: fractons
    • L 625–631
    • Alexander, S. & Orbach, R. (1982). Density of states on fractals: fractons. J. Phys. Lett. 43, L 625–631.
    • (1982) J. Phys. Lett , vol.43
    • Alexander, S.1    Orbach, R.2
  • 9
    • 0001661973 scopus 로고
    • Molecular dynamics of hydrocarbon molecules in condensed phases. II. Benzene
    • 4078–4089
    • Anderson, J., Ullo, J. J. & Yip, S. (1987). Molecular dynamics of hydrocarbon molecules in condensed phases. II. Benzene. J. chem. Phys. 86 (7), 4078–4089.
    • (1987) J. chem. Phys , vol.86 , Issue.7
    • Anderson, J.1    Ullo, J.J.2    Yip, S.3
  • 10
    • 0022419296 scopus 로고
    • A molecular dynamics study of the C-terminal fragment of the L7/L12 ribosomal protein. Secondary structure motion in a 150 picosecond trajectory
    • 461–477
    • Aqvist, J., Van Gunsteren, W. F., Leijonmarck, M. & Tapia, O. (1985). A molecular dynamics study of the C-terminal fragment of the L7/L12 ribosomal protein. Secondary structure motion in a 150 picosecond trajectory, J. molec. Biol. 183, 461–477.
    • (1985) J. molec. Biol. 183
    • Aqvist, J.1    Van Gunsteren, W.F.2    Leijonmarck, M.3    Tapia, O.4
  • 11
    • 0018447854 scopus 로고
    • Far-infrared spectrum of crystalline lysozyme
    • 507–516
    • Ataka, M. & Tanaka, S. (1979). Far-infrared spectrum of crystalline lysozyme. Biopolymers 18, 507–516.
    • (1979) Biopolymers , vol.18
    • Ataka, M.1    Tanaka, S.2
  • 12
    • 36849101322 scopus 로고
    • Inelastic neutron scattering study of the ‘rotator’ phase transition in n-nonadecane
    • 5193–201
    • Barnes, J. D. (1973). Inelastic neutron scattering study of the ‘rotator’ phase transition in n-nonadecane. J. chem, Phys. 58, 5193–201.
    • (1973) J. chem, Phys. 58
    • Barnes, J.D.1
  • 13
    • 0020014744 scopus 로고
    • Intramolecular low-frequency vibrations in lysozyme by neutron time-of-flight spectroscopy
    • 43–50
    • Bartunik, H. D., Jolles, P., Berthou, J. & Dianoux, A. J. (1982). Intramolecular low-frequency vibrations in lysozyme by neutron time-of-flight spectroscopy. Biopolymers 21, 43–50.
    • (1982) Biopolymers , vol.21
    • Bartunik, H.D.1    Jolles, P.2    Berthou, J.3    Dianoux, A.J.4
  • 14
    • 84983898524 scopus 로고
    • Inelastic nature of the diffuse X-ray scattering near the α-β transition in quartz
    • B 48, 437–443
    • Bauer, K., Jagodzinski, H., Dorner, B. & Grimm, H. (1971). Inelastic nature of the diffuse X-ray scattering near the α-β transition in quartz. Physica Status Solidi B 48, 437–443.
    • (1971) Physica Status Solidi
    • Bauer, K.1    Jagodzinski, H.2    Dorner, B.3    Grimm, H.4
  • 16
    • 0020069482 scopus 로고
    • Study of storage iron in cultured chick embryo fibroblasts and rat glioma cells, using Moessbauer spectroscopy
    • 133–140
    • Bauminger, E. R., Cohen, S. G., Ofer, S. & Bachrach, U. (1982). Study of storage iron in cultured chick embryo fibroblasts and rat glioma cells, using Moessbauer spectroscopy. Biochim. biophys. Acta 720, 133–140.
    • (1982) Biochim. biophys. Acta , vol.720
    • Bauminger, E.R.1    Cohen, S.G.2    Ofer, S.3    Bachrach, U.4
  • 17
    • 0003952816 scopus 로고
    • Quasielastic Neutron Scattering: Principles and Applications in Solid State Chemistry, Biology and Materials Science
    • Bristol and Philadelphia: Adam Hilger.
    • Bee, M. (1988). Quasielastic Neutron Scattering: Principles and Applications in Solid State Chemistry, Biology and Materials Science. Bristol and Philadelphia: Adam Hilger.
    • (1988)
    • Bee, M.1
  • 18
    • 0017090583 scopus 로고
    • The low-frequency vibrational modes of an RNA: Poly(I)-Poly(C)
    • 2299–2301
    • Beetz, C. A. & Ascarelli, G. (1976). The low-frequency vibrational modes of an RNA: Poly(I)-Poly(C). Biopolymers 15, 2299–2301.
    • (1976) Biopolymers , vol.15
    • Beetz, C.A.1    Ascarelli, G.2
  • 19
    • 0020383099 scopus 로고
    • Far-infrared absorption of nucleotides and Poly(I).Poly(C) RNA
    • 1569–1586
    • Beetz, C. A. & Ascarelli, G. (1982). Far-infrared absorption of nucleotides and Poly(I).Poly(C) RNA. Biopolymers 21, 1569–1586.
    • (1982) Biopolymers , vol.21
    • Beetz, C.A.1    Ascarelli, G.2
  • 20
    • 36549093328 scopus 로고
    • Locating transition states
    • 2464–2475
    • Bell, S. & Crichton, J. S. (1984). Locating transition states. J. chem. Phys. 80, 2464–2475.
    • (1984) J. chem. Phys , vol.80
    • Bell, S.1    Crichton, J.S.2
  • 22
    • 0010504069 scopus 로고
    • Dynamics of supercooled liquids and the glass transition
    • 5915–5934
    • Bengtzelius, U., Gotze, W. & Sjolander, A. (1984). Dynamics of supercooled liquids and the glass transition. J, Phys. C 17, 5915–5934.
    • (1984) J, Phys. C , vol.17
    • Bengtzelius, U.1    Gotze, W.2    Sjolander, A.3
  • 23
    • 0019201173 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer
    • 211–230
    • Bennett, W. S. & Steitz, T. A. (1980). Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer, J. molec. Biol. 140, 211–230.
    • (1980) J. molec. Biol. 140
    • Bennett, W.S.1    Steitz, T.A.2
  • 24
    • 9144274435 scopus 로고
    • Molecular dynamics and spectra. 1. Diatomic rotation and vibration
    • 4872–4882
    • Berens, P. H. & Wilson, K. R. (1981). Molecular dynamics and spectra. 1. Diatomic rotation and vibration. J. chem. Phys. 74 (9), 4872–4882.
    • (1981) J. chem. Phys , vol.74 , Issue.9
    • Berens, P.H.1    Wilson, K.R.2
  • 25
    • 0023388073 scopus 로고
    • Collagen; an inelastic neutron scattering study of low-frequency vibrational modes
    • 343–345
    • Berney, C. V., Renugopalakrishnan, V. & Bhatnagar. (1987). Collagen; an inelastic neutron scattering study of low-frequency vibrational modes. Biophys. J. 52, 343–345.
    • (1987) Biophys. J , vol.52
    • Berney, C.V.1    Renugopalakrishnan, V.2    Bhatnagar3
  • 26
    • 0022372682 scopus 로고
    • Do vibrational spectroscopies uniquely describe protein dynamics? The case for myoglobin
    • 1027–1044
    • Bialek, W. & Goldstein, R. F. (1985). Do vibrational spectroscopies uniquely describe protein dynamics? The case for myoglobin. Biophys. J. 48, 1027–1044.
    • (1985) Biophys. J , vol.48
    • Bialek, W.1    Goldstein, R.F.2
  • 27
    • 0022429109 scopus 로고
    • Dielectric studies of protein hydration and hydration-induced flexibility
    • 323–326
    • Bone, S. & Pethig, R. (1985). Dielectric studies of protein hydration and hydration-induced flexibility. J. molec. Biol. 181, 323–326.
    • (1985) J. molec. Biol , vol.181
    • Bone, S.1    Pethig, R.2
  • 28
    • 0004271613 scopus 로고
    • Molecular Hydrodynamics
    • New York McGraw-Hill.
    • Boon, J. P. & Yip, S. (1980). Molecular Hydrodynamics. New York: McGraw-Hill.
    • (1980)
    • Boon, J.P.1    Yip, S.2
  • 29
    • 0000001019 scopus 로고
    • Thermodynamics of ionic solvation: the influence of long-range truncation on the thermodynamics of aqueous ionic solutions
    • 5156–5162
    • Brooks, C. L. (1987). Thermodynamics of ionic solvation: the influence of long-range truncation on the thermodynamics of aqueous ionic solutions. J. chem. Phys. 86, 5156–5162.
    • (1987) J. chem. Phys , vol.86
    • Brooks, C.L.1
  • 30
    • 0000991642 scopus 로고
    • Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor
    • 6571-6575
    • Brooks, B. & Karplus, M. (1983). Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor. Proc. natn. Acad. Sci. U.S.A. 80, 6571-6575.
    • (1983) Proc. natn. Acad. Sci. U.S.A. 80
    • Brooks, B.1    Karplus, M.2
  • 31
    • 0022111715 scopus 로고
    • Normal modes for specific motions of macromolecules: application to the hinge-bending motion of lysozyme
    • 4995–4999
    • Brooks, B. & Karplus, M. (1985). Normal modes for specific motions of macromolecules: application to the hinge-bending motion of lysozyme. Proc. natn. Acad. Sci. U.S.A. 82, 4995–4999.
    • (1985) Proc. natn. Acad. Sci. U.S.A , vol.82
    • Brooks, B.1    Karplus, M.2
  • 32
    • 0024354001 scopus 로고
    • Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme
    • 159–181
    • Brooks, C. L. & Karplus, M. (1989). Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme. J. molec. Biol. 208, 159–181.
    • (1989) J. molec. Biol. 208
    • Brooks, C.L.1    Karplus, M.2
  • 34
    • 0001031179 scopus 로고
    • Proteins. A theoretical perspective of dynamics, structure and thermodynamics
    • (Eds. I. Prigogine & S. Rice) Wiley.
    • Brooks, C. L. III, Karplus, M. & Pettitt, B. M. (1988). Proteins. A theoretical perspective of dynamics, structure and thermodynamics. Adv. chem. Physics 71, (Eds. I. Prigogine & S. Rice) Wiley.
    • (1988) Adv. chem. Physics , vol.71
    • Brooks, C.L.1    Karplus, M.2    Pettitt, B.M.3
  • 35
    • 26744440015 scopus 로고
    • Structural and energetic effects of truncating long-range interactions in polar fluids
    • 5897–5908
    • Brooks, C. L. III, Pettitt, B. M. & Karplus, M. (1985). Structural and energetic effects of truncating long-range interactions in polar fluids. J. chem. Phys. 83, 5897–5908.
    • (1985) J. chem. Phys , vol.83
    • Brooks, C.L.1    Pettitt, B.M.2    Karplus, M.3
  • 36
    • 0015353157 scopus 로고
    • Conformationally dependent low-frequency motions of proteins by laser Raman spectroscopy
    • 1467—1469
    • Brown, R. G., Erfurth, S. C., Small, E. W. & Peticolas, W. L. (1972). Conformationally dependent low-frequency motions of proteins by laser Raman spectroscopy. Proc. natn. Acad. Sci. U.S.A. 69 (6), 1467—1469.
    • (1972) Proc. natn. Acad. Sci. U.S.A , vol.69 , Issue.6
    • Brown, R.G.1    Erfurth, S.C.2    Small, E.W.3    Peticolas, W.L.4
  • 37
    • 0022780988 scopus 로고
    • The hinge-bending mode of a lysozyme-inhibitor complex
    • 1767—1802
    • Bruccoleri, R. E., Karplus, M. & McCammon, J. A. (1986). The hinge-bending mode of a lysozyme-inhibitor complex. Biopolymers 25, 1767—1802.
    • (1986) Biopolymers , vol.25
    • Bruccoleri, R.E.1    Karplus, M.2    McCammon, J.A.3
  • 38
    • 0004151408 scopus 로고
    • Molecular Mechanics
    • ACS monograph. American Chemical Society.
    • Burkert, U. & Allinger, N. (1982). Molecular Mechanics. ACS monograph. American Chemical Society.
    • (1982)
    • Burkert, U.1    Allinger, N.2
  • 39
    • 0023640468 scopus 로고
    • Linkage of functional and structural heterogeneity in proteins: Dynamic hole burning in carboxymyoglobin
    • 373–376
    • Campbell, B. F., Chance, M. R. & Friedman, J. M. (1987). Linkage of functional and structural heterogeneity in proteins: Dynamic hole burning in carboxymyoglobin. Science, Wash. 238, 373–376.
    • (1987) Science, Wash. 238
    • Campbell, B.F.1    Chance, M.R.2    Friedman, J.M.3
  • 40
    • 0012656405 scopus 로고
    • Structures and energetics of proteins and their active sites
    • 55–107
    • Campbell, I. D., Dobson, C. M. & Williams, R. J. P. (1978). Structures and energetics of proteins and their active sites. Adv. chem. Phys. 39, 55–107.
    • (1978) Adv. chem. Phys , vol.39
    • Campbell, I.D.1    Dobson, C.M.2    Williams, R.J.P.3
  • 43
    • 0348251690 scopus 로고
    • Molecular vibrations in glassy glycerol measured by Moessbauer scattering
    • 1276–1284
    • Champeney, D. C. & Dean, C. W. (1975). Molecular vibrations in glassy glycerol measured by Moessbauer scattering. J. Phys. C 8, 1276–1284.
    • (1975) J. Phys. C , vol.8
    • Champeney, D.C.1    Dean, C.W.2
  • 44
    • 0020730848 scopus 로고    scopus 로고
    • Low-frequency vibrations of helical structures in protein molecules
    • (1983 a) 573–580
    • Chou, K. C. (1983 a). Low-frequency vibrations of helical structures in protein molecules. Biochem. J. 209, 573–580.
    • Biochem. J , vol.209
    • Chou, K.C.1
  • 45
    • 0021007144 scopus 로고    scopus 로고
    • Identification of low-frequency modes in protein molecules
    • (1983 6) 465–469
    • Chou, K. C. (1983 6). Identification of low-frequency modes in protein molecules. Biochem. J. 215, 465–469.
    • Biochem. J , vol.215
    • Chou, K.C.1
  • 46
    • 0021245237 scopus 로고
    • Biological functions of low-frequency vibrations (phonons). III. Helical structures and microenvironment. Biophys. J. 45, 881–890
    • Chou, K. C. (1984). Biological functions of low-frequency vibrations (phonons). III. Helical structures and microenvironment. Biophys. J. 45, 881–890.
    • (1984)
    • Chou, K.C.1
  • 47
    • 0003564877 scopus 로고
    • MOTECC: Modern Techniques in Computational Chemistry
    • (Ed. E. Clementi). Escom: Leiden.
    • Clementi, E., Corongiu, G., Aida, M., Niesar, V. & Kneller, G. (1990). In ‘MOTECC: Modern Techniques in Computational Chemistry’ (Ed. E. Clementi). Escom: Leiden.
    • (1990)
    • Clementi, E.1    Corongiu, G.2    Aida, M.3    Niesar, V.4    Kneller, G.5
  • 48
    • 0000668262 scopus 로고
    • Dynamics of the iron-containing core in crystals of the iron-storage protein, ferritin, through Moessbauer spectroscopy
    • 1244–1248
    • Cohen, S. G., Bauminger, E. R., Nowik, I., Ofer, S. & Yariv, J. (1981). Dynamics of the iron-containing core in crystals of the iron-storage protein, ferritin, through Moessbauer spectroscopy. Phys. Rev. Lett. 46, 1244–1248.
    • (1981) Phys. Rev. Lett , vol.46
    • Cohen, S.G.1    Bauminger, E.R.2    Nowik, I.3    Ofer, S.4    Yariv, J.5
  • 49
    • 36849108849 scopus 로고
    • Molecular Schrodinger equation. VIII. A new method for the evaluation of multidimensional integrals
    • 5307–5318
    • Conroy, H. (1967). Molecular Schrodinger equation. VIII. A new method for the evaluation of multidimensional integrals. J. chem. Phys. 47 (12), 5307–5318.
    • (1967) J. chem. Phys , vol.47 , Issue.12
    • Conroy, H.1
  • 50
    • 85040204257 scopus 로고
    • Structural Dynamics
    • New York Wiley.
    • Craig, R. R. (1981). Structural Dynamics. New York: Wiley.
    • (1981)
    • Craig, R.R.1
  • 53
    • 0011443092 scopus 로고
    • Low frequency motion in proteins and its study by inelastic neutron scattering
    • 243–271
    • Cusack, S. (1986). Low frequency motion in proteins and its study by inelastic neutron scattering. Comm. molec. cell. Biophys. 3 (4), 243–271.
    • (1986) Comm. molec. cell. Biophys , vol.3 , Issue.4
    • Cusack, S.1
  • 55
    • 0025333959 scopus 로고
    • Temperature dependence of the low frequency dynamics of myoglobin. Measurement of the vibrational frequency distribution by inelastic neutron scattering
    • 243–251
    • Cusack, S. & Doster, W. (1990). Temperature dependence of the low frequency dynamics of myoglobin. Measurement of the vibrational frequency distribution by inelastic neutron scattering. Biophys. J. 58, 243–251.
    • (1990) Biophys. J , vol.58
    • Cusack, S.1    Doster, W.2
  • 56
    • 46149138166 scopus 로고
    • Low frequency dynamics of proteins studied by neutron time-of-flight spectroscopy
    • 136 B, 256–259
    • Cusack, S., Smith, J., Finney, J., Karplus, M. & Trewhella, J. (1986). Low frequency dynamics of proteins studied by neutron time-of-flight spectroscopy. Physica 136 B, 256–259.
    • (1986) Physica
    • Cusack, S.1    Smith, J.2    Finney, J.3    Karplus, M.4    Trewhella, J.5
  • 58
    • 0024722571 scopus 로고
    • Reaction path study of conformational transitions and helix formation in a tetrapeptide
    • 6963–6967
    • Czerminski, R. & Elber, R. (1989). Reaction path study of conformational transitions and helix formation in a tetrapeptide. Proc. natn. Acad. Sci. U.S.A. 86, 6963–6967.
    • (1989) Proc. natn. Acad. Sci. U.S.A , vol.86
    • Czerminski, R.1    Elber, R.2
  • 59
    • 0042487854 scopus 로고
    • Neutron scattering from a quantum oscillator subject to noise
    • 1034–1038
    • Dattagupta, S. & Reiter, G. F. (1985). Neutron scattering from a quantum oscillator subject to noise. Phys. Rev. A 31 (2), 1034–1038.
    • (1985) Phys. Rev. A , vol.31 , Issue.2
    • Dattagupta, S.1    Reiter, G.F.2
  • 60
    • 0006042593 scopus 로고
    • Dielectric relaxation in glycerol
    • 1417–1419
    • Davidson, D. W. & Cole, R. H. (1950). Dielectric relaxation in glycerol.J. chem. Phys. 18, 1417–1419.
    • (1950) J. chem. Phys , vol.18
    • Davidson, D.W.1    Cole, R.H.2
  • 61
    • 84978673769 scopus 로고
    • Zur Theorie der spezifischen Warmen
    • 789–839
    • Debye, P. (1912). Zur Theorie der spezifischen Warmen. Annln Phys. 39, 789–839.
    • (1912) Annln Phys , vol.39
    • Debye, P.1
  • 62
    • 0000072333 scopus 로고
    • Dynamics of molecular impurities in crystals
    • B 19, 767–782
    • De Raedt, B. & Michel, K. H. (1979). Dynamics of molecular impurities in crystals. Phys. Rev. B 19, 767–782.
    • (1979) Phys. Rev
    • De Raedt, B.1    Michel, K.H.2
  • 63
    • 0017516652 scopus 로고
    • The problem of orientational order in tilted smectic phases: a high resolution neutron quasi elastic study
    • 809–816
    • Dianoux, A. J., Hervet, H. & Volino, F. (1977). The problem of orientational order in tilted smectic phases: a high resolution neutron quasi elastic study. J. Phys., Paris 38, 809–816.
    • (1977) J. Phys., Paris , vol.38
    • Dianoux, A.J.1    Hervet, H.2    Volino, F.3
  • 64
    • 0001520102 scopus 로고
    • Incoherent scattering law for neutron quasielastic scattering in liquid crystals
    • 1181–1194
    • Dianoux, A. J., Volino, F. & Hervet, H. (1975). Incoherent scattering law for neutron quasielastic scattering in liquid crystals. Molec. Phys. 20, 1181–1194.
    • (1975) Molec. Phys , vol.20
    • Dianoux, A.J.1    Volino, F.2    Hervet, H.3
  • 65
    • 0022555890 scopus 로고
    • Internal motion in proteins: Nuclear magnetic resonance measurements and dynamic simulations
    • 362–389
    • Dobson, C. M. & Karplus, M. (1986). Internal motion in proteins: Nuclear magnetic resonance measurements and dynamic simulations. Meth. Enzym. 131, 362–389.
    • (1986) Meth. Enzym , vol.131
    • Dobson, C.M.1    Karplus, M.2
  • 66
    • 0003848679 scopus 로고
    • Coherent inelastic neutron scattering in lattice dynamics
    • Heidelberg Springer-Verlag.
    • Dorner, B. (1982). Coherent inelastic neutron scattering in lattice dynamics. In Tracts in Modern Physics, vol. 93. Heidelberg: Springer-Verlag.
    • (1982) Tracts in Modern Physics , vol.93
    • Dorner, B.1
  • 67
    • 0024808136 scopus 로고
    • On the mechanism of ligand binding to myoglobin. The role of structural fluctuations
    • 217–220
    • Doster, W. (1989). On the mechanism of ligand binding to myoglobin. The role of structural fluctuations. Eur. Biophys. J. 17, 217–220.
    • (1989) Eur. Biophys. J. 17
    • Doster, W.1
  • 68
    • 0022762471 scopus 로고
    • Thermal properties of water in myoglobin crystals and solutions at subzero temperatures
    • 213–219
    • Doster, W., Bachleitner, A., Dunau, R., Hiebl, M. & Luscher, E. (1986). Thermal properties of water in myoglobin crystals and solutions at subzero temperatures. Biophys. J. 50, 213–219.
    • (1986) Biophys. J , vol.50
    • Doster, W.1    Bachleitner, A.2    Dunau, R.3    Hiebl, M.4    Luscher, E.5
  • 69
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature, Lond
    • 754–756
    • Doster, W., Cusack, S. & Petry, W. (1989). Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature, Lond. 337, 754–756.
    • (1989) , vol.337
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 70
    • 0001706226 scopus 로고
    • Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering
    • 1080–1083
    • Doster, W., Cusack, S. & Petry, W. (1990). Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering. Phys. Rev. Lett. 65 (8), 1080–1083.
    • (1990) Phys. Rev. Lett , vol.65 , Issue.8
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 71
    • 0023115053 scopus 로고
    • Molecular dynamics studied by analysis of the X-ray diffuse scattering from lysozyme crystals
    • Lond. 190–192
    • Doucet, J. Benoit, J. P. (1987). Molecular dynamics studied by analysis of the X-ray diffuse scattering from lysozyme crystals. Nature, Lond. 337, 190–192.
    • (1987) Nature , vol.337
    • Doucet, J.1    Benoit, J.P.2
  • 72
    • 0016735247 scopus 로고
    • Neutron scattering spectroscopy of the a-and β-forms of poly-L-alanine. Motion of the methyl side chain
    • 715–721
    • Drexel, W. & Peticolas, W. L. (1978). Neutron scattering spectroscopy of the a-and β-forms of poly-L-alanine. Motion of the methyl side chain. Biopolymers 14, 715–721.
    • (1978) Biopolymers 14
    • Drexel, W.1    Peticolas, W.L.2
  • 73
    • 33845278689 scopus 로고
    • Interpretation of atomic displacement parameters form diffraction studies of crystals
    • 856–867
    • Dunitz, J. D., Schomaker, V. & Trueblood, K. N. (1988). Interpretation of atomic displacement parameters form diffraction studies of crystals. J. phys. Chem. 92 (4), 856–867.
    • (1988) J. phys. Chem , vol.92 , Issue.4
    • Dunitz, J.D.1    Schomaker, V.2    Trueblood, K.N.3
  • 74
    • 0017869404 scopus 로고
    • Water and Proteins. I. The significance and structure of water; its interaction with electrolytes and non-electrolytes
    • Edsall, J. T. & Mackenzie, H. A. (1978), Water and Proteins. I. The significance and structure of water; its interaction with electrolytes and non-electrolytes. Adv. Biophys. 10, 137.
    • (1978) Adv. Biophys. 10, 137
    • Edsall, J.T.1    Mackenzie, H.A.2
  • 75
    • 49049126268 scopus 로고
    • Water and Proteins II. The location and dynamics of water in protein systems and its relation to their stability and properties
    • 53–183
    • Edsall, J. T. & Mackenzie, H. A. (1983). Water and Proteins II. The location and dynamics of water in protein systems and its relation to their stability and properties. Adv. Biophys. 16, 53–183.
    • (1983) Adv. Biophys , vol.16
    • Edsall, J.T.1    Mackenzie, H.A.2
  • 76
    • 0000438948 scopus 로고
    • Calculation of the potential of mean force using molecular dynamics with linear constraints: an application to a conformational transition in a solvated dipeptide
    • 4312–4321
    • Elber, R. (1990). Calculation of the potential of mean force using molecular dynamics with linear constraints: an application to a conformational transition in a solvated dipeptide. J. chem. Phys. 93 (6), 4312–4321.
    • (1990) J. chem. Phys , vol.93 , Issue.6
    • Elber, R.1
  • 77
    • 0001058199 scopus 로고
    • Low-frequency modes in proteins: use of the effective-medium approximation to interpret the fractal dimension observed in electron-spin relaxation measurements
    • 394—397
    • Elber, R. & Karplus, M. (1986). Low-frequency modes in proteins: use of the effective-medium approximation to interpret the fractal dimension observed in electron-spin relaxation measurements. Phys. Rev. Letts. 56 (4), 394—397.
    • (1986) Phys. Rev. Letts , vol.56 , Issue.4
    • Elber, R.1    Karplus, M.2
  • 78
    • 0023140044 scopus 로고    scopus 로고
    • Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin
    • (1987a) 318—321
    • Elber, R. & Karplus, M. (1987a). Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin. Science, Wash. 235, 318—321.
    • Science, Wash , vol.235
    • Elber, R.1    Karplus, M.2
  • 79
    • 0000603016 scopus 로고    scopus 로고
    • A method for determining reaction paths in large molecules: Application to myoglobin
    • (1987b) 375–380
    • Elber, R. & Karplus, M. (1987b). A method for determining reaction paths in large molecules: Application to myoglobin. Chem. Phys. Letts. 139, 375–380.
    • Chem. Phys. Letts , vol.139
    • Elber, R.1    Karplus, M.2
  • 80
    • 0001689772 scopus 로고
    • Protein hydration and enzyme activity: The role of hydration-induced conformation and dynamic changes in the activity of lysozyme
    • 129–151
    • Finney, J. L. & Poole, P. L. (1984). Protein hydration and enzyme activity: The role of hydration-induced conformation and dynamic changes in the activity of lysozyme. Comments molec. Cell. Biophys. 2, 129–151.
    • (1984) Comments molec. Cell. Biophys , vol.2
    • Finney, J.L.1    Poole, P.L.2
  • 82
    • 0018793861 scopus 로고
    • Temperature dependent X-ray diffraction as a probe of protein structural dynamics
    • 558–563
    • Frauenfelder, H., Petsko, G. & Tsernoglou, D. (1979). Temperature dependent X-ray diffraction as a probe of protein structural dynamics. Nature, Lond. 280, 558–563.
    • (1979) Nature, Lond. 280
    • Frauenfelder, H.1    Petsko, G.2    Tsernoglou, D.3
  • 83
    • 0021796467 scopus 로고
    • Rate theories and puzzles in heme-protein kinetics
    • 337–345
    • Frauenfelder, H. & Wolynes, P. (1985). Rate theories and puzzles in heme-protein kinetics. Science, Wash. 229, 337–345.
    • (1985) Science, Wash. 229
    • Frauenfelder, H.1    Wolynes, P.2
  • 84
    • 33746150090 scopus 로고
    • Study of the glass transition order parameter in amorphous polybutadiene by incoherent neutron scattering
    • B 70, 73–79
    • Frick, B., Richter, D., Petry, W. & Buchenau, U. (1988). Study of the glass transition order parameter in amorphous polybutadiene by incoherent neutron scattering. Z. Phys. B 70, 73–79.
    • (1988) Z. Phys
    • Frick, B.1    Richter, D.2    Petry, W.3    Buchenau, U.4
  • 85
    • 0343757149 scopus 로고
    • Harmonic vibrations and thermodynamic stability of a DNA oligomer on monovalent salt solution
    • 3160–3164
    • Garcia, A. E. & Soumpasis, D. M. (1989). Harmonic vibrations and thermodynamic stability of a DNA oligomer on monovalent salt solution. Proc. natn. Acad. Sci. U.S.A. 86, 3160–3164.
    • (1989) Proc. natn. Acad. Sci. U.S.A , vol.86
    • Garcia, A.E.1    Soumpasis, D.M.2
  • 87
    • 0020789212 scopus 로고
    • Relaxation processes on a picosecond timescale in hemoglobin and poly(L-alanine)
    • 1715–1729
    • Genzel, L., Kremer, F., Poglitsch, A. & Bechtold, G. (1983). Relaxation processes on a picosecond timescale in hemoglobin and poly(L-alanine). Biopolymers 22, 1715–1729.
    • (1983) Biopolymers , vol.22
    • Genzel, L.1    Kremer, F.2    Poglitsch, A.3    Bechtold, G.4
  • 88
    • 0014116254 scopus 로고
    • Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide
    • 420–427
    • Gibson, K. D. & Scheraga, H. A. (1967). Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide. Proc. natn. Acad. Sci. U.S.A. 58, 420–427.
    • (1967) Proc. natn. Acad. Sci. U.S.A , vol.58
    • Gibson, K.D.1    Scheraga, H.A.2
  • 89
    • 0041375129 scopus 로고
    • Quasielastic and inelastic neutron scattering in macromolecular solutions
    • 689–696
    • Giordano, R., Salvato, G., Wanderlingh, F. & Wanderlingh, U. (1990). Quasielastic and inelastic neutron scattering in macromolecular solutions. Phys. Rev. A 41 (2), 689–696.
    • (1990) Phys. Rev. A , vol.41 , Issue.2
    • Giordano, R.1    Salvato, G.2    Wanderlingh, F.3    Wanderlingh, U.4
  • 90
    • 0025064089 scopus 로고
    • A theorem on amplitudes of thermal atomic fluctuations in large molecules assuming specific conformations calculated by normal mode analysis
    • 105–112
    • Go, N. (1990). A theorem on amplitudes of thermal atomic fluctuations in large molecules assuming specific conformations calculated by normal mode analysis. Biophys. Chem. 35, 105–112.
    • (1990) Biophys. Chem , vol.35
    • Go, N.1
  • 91
    • 0020771265 scopus 로고
    • Dynamics of a small globular protein in terms of low-frequency vibrational modes
    • 3696–3700
    • Go, N., Noguti, T. & Nishikawa, T. (1983). Dynamics of a small globular protein in terms of low-frequency vibrational modes. Proc. natn. Acad. Sci. U.S.A. 80, 3696–3700.
    • (1983) Proc. natn. Acad. Sci. U.S.A , vol.80
    • Go, N.1    Noguti, T.2    Nishikawa, T.3
  • 92
    • 0024952939 scopus 로고
    • Protein and protein-bound water dynamics studied by Rayleigh scattering of Moessbauer radiation (RSMR)
    • 39–92
    • Goldanskii, V. & Krupyanskii, Y. F. (1989). Protein and protein-bound water dynamics studied by Rayleigh scattering of Moessbauer radiation (RSMR). Q. Rev. Biophys. 22 (1), 39–92.
    • (1989) Q. Rev. Biophys , vol.22 , Issue.1
    • Goldanskii, V.1    Krupyanskii, Y.F.2
  • 93
    • 85012573032 scopus 로고
    • Correlation functions for molecular motion
    • 1-42
    • Gordon, R. G. (1968). Correlation functions for molecular motion. Adv. Mag. Reson. 3, 1-42.
    • (1968) Adv. Mag. Reson , vol.3
    • Gordon, R.G.1
  • 94
    • 36749119748 scopus 로고
    • Energy diffusion-controlled reactions in solution
    • 3736-3743
    • Grote, R. F. & Hynes, J. T. (1982). Energy diffusion-controlled reactions in solution. J. chem. Phys. 77, 3736-3743.
    • (1982) J. chem. Phys , vol.77
    • Grote, R.F.1    Hynes, J.T.2
  • 95
    • 0021701376 scopus 로고
    • Variational calculation of the normal modes of a large macromolecule: methods and some initial results
    • 2943–2949
    • Harrison, R. W. (1984). Variational calculation of the normal modes of a large macromolecule: methods and some initial results. Biopolymers 23, 2943–2949.
    • (1984) Biopolymers , vol.23
    • Harrison, R.W.1
  • 98
    • 0024519351 scopus 로고
    • Treatment of electrostatic effects in macromolecular modelling
    • 78–92
    • Harvey, S. C. (1989). Treatment of electrostatic effects in macromolecular modelling. Proteins: Struct. Funct. Genetics 5, 78–92.
    • (1989) Proteins: Struct. Funct. Genetics , vol.5
    • Harvey, S.C.1
  • 99
    • 0041179806 scopus 로고
    • Picosecond fluorescence decay of tryptophans in myoglobin
    • 4399–4403
    • Hochstrasser, R. M. & Negus D. K. (1984). Picosecond fluorescence decay of tryptophans in myoglobin. Proc. natn. Acad. Sci. U.S.A. 81, 4399–4403.
    • (1984) Proc. natn. Acad. Sci. U.S.A , vol.81
    • Hochstrasser, R.M.1    Negus, D.K.2
  • 100
    • 0014836942 scopus 로고
    • The basic trypsin inhibitor of bovine pancreas. 1. Structure analysis and conformation of the polypeptide chain
    • 389–392
    • Huber, R., Kukla, D., Ruhlmann, A., Epp, O. & Formanek, H. (1970). The basic trypsin inhibitor of bovine pancreas. 1. Structure analysis and conformation of the polypeptide chain. Naturwissenschaften 57, 389–392.
    • (1970) Naturwissenschaften , vol.57
    • Huber, R.1    Kukla, D.2    Ruhlmann, A.3    Epp, O.4    Formanek, H.5
  • 101
    • 0025675240 scopus 로고
    • T4 phage lysozyme: a protein designed for understanding tryptophan photophysics
    • (ed. J. R. Lakowicz, M. R. Eftink, T. M. Nordlund, J. B. A. Ross and R. F. Steiner). SPIE. Vol. 124, pp. 80–91
    • Hudson, B. S. & Harris, D. (1990). T4 phage lysozyme: a protein designed for understanding tryptophan photophysics. In Time-resolved Laser Spectroscopy in Biochemistry II (ed. J. R. Lakowicz, M. R. Eftink, T. M. Nordlund, J. B. A. Ross and R. F. Steiner). SPIE. Vol. 124, pp. 80–91.
    • (1990) Time-resolved Laser Spectroscopy in Biochemistry II
    • Hudson, B.S.1    Harris, D.2
  • 102
    • 84959711805 scopus 로고
    • Fluoresence anisotropy decay determinations of rapid reorientational motion: Complications in the interpretation of bilayer acyl-chain and protein tryptophan dynamics
    • 171—188
    • Hudson, B. S., Ludescher, R. D., Ruggiero, A., Harris, D. L. & Johnson, I. (1987). Fluoresence anisotropy decay determinations of rapid reorientational motion: Complications in the interpretation of bilayer acyl-chain and protein tryptophan dynamics. Comm. molec. cell. Biophys. 4, 171—188.
    • (1987) Comm. molec. cell. Biophys , vol.4
    • Hudson, B.S.1    Ludescher, R.D.2    Ruggiero, A.3    Harris, D.L.4    Johnson, I.5
  • 103
    • 0040297591 scopus 로고
    • Molecular inelastic neutron scattering: computational methods using consistent force fields
    • 2930-2939
    • Hudson, B., Warshel, A. & Gordon, R. G. (1974). Molecular inelastic neutron scattering: computational methods using consistent force fields. J. chem. Phys. 61 (7), 2930-2939.
    • (1974) J. chem. Phys , vol.61 , Issue.7
    • Hudson, B.1    Warshel, A.2    Gordon, R.G.3
  • 104
    • 0021096858 scopus 로고
    • Fluorescence depolarisation of tryptophan residues in proteins: a molecular dynamics study
    • 2884–2893
    • Ichiye, T. & Karplus, M. (1983). Fluorescence depolarisation of tryptophan residues in proteins: a molecular dynamics study. Biochemistry 22, 2884–2893.
    • (1983) Biochemistry , vol.22
    • Ichiye, T.1    Karplus, M.2
  • 105
    • 0023512803 scopus 로고
    • Anisotropy and anharmonicity of atomic fluctuations in proteins: analysis of a molecular dynamics simulation
    • 236–259
    • Ichiye, T. & Karplus, M. (1987). Anisotropy and anharmonicity of atomic fluctuations in proteins: analysis of a molecular dynamics simulation. Proteins: Struct. Funct. Genet. 2, 236–259.
    • (1987) Proteins: Struct. Funct. Genet , vol.2
    • Ichiye, T.1    Karplus, M.2
  • 106
    • 0024276807 scopus 로고
    • Anisotropy and anharmonicity of atomic fluctuations in proteins: implications for X-ray analysis
    • 3487–3497
    • Ichiye, T. & Karplus, M. (1988). Anisotropy and anharmonicity of atomic fluctuations in proteins: implications for X-ray analysis. Biochemistry 27, 3487–3497.
    • (1988) Biochemistry , vol.27
    • Ichiye, T.1    Karplus, M.2
  • 107
    • 0019913548 scopus 로고
    • Inelastic neutron scattering analysis of hexokinase and its modification on binding of glucose
    • 85–86
    • Jacrot, B., Cusack, S., Dianoux, A. J. & Engelman, D. M. (1982). Inelastic neutron scattering analysis of hexokinase and its modification on binding of glucose. Nature, Lond. 300, 85–86.
    • (1982) Nature, Lond , vol.300
    • Jacrot, B.1    Cusack, S.2    Dianoux, A.J.3    Engelman, D.M.4
  • 108
    • 0000629803 scopus 로고
    • Dynamics of nonadiabatic atom transfer in biological systems. Carbon monoxide binding to hemoglobin
    • 3744-3754
    • Jortner, J. & Ulstrup, J. (1979). Dynamics of nonadiabatic atom transfer in biological systems. Carbon monoxide binding to hemoglobin. J. Am. Chem. Soc. 101 (14), 3744-3754.
    • (1979) J. Am. Chem. Soc , vol.101 , Issue.14
    • Jortner, J.1    Ulstrup, J.2
  • 109
    • 0000127140 scopus 로고
    • Method for estimating the configurational entropy of macromolecules
    • 325–332
    • Karplus, M. & Kushick, J. (1981). Method for estimating the configurational entropy of macromolecules. Macromolecules 14, 325–332.
    • (1981) Macromolecules , vol.14
    • Karplus, M.1    Kushick, J.2
  • 110
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • 631–639
    • Karplus, M. & Petsko, G. (1990). Molecular dynamics simulations in biology. Nature, Lond. 347, 631–639.
    • (1990) Nature, Lond , vol.347
    • Karplus, M.1    Petsko, G.2
  • 111
    • 0004236128 scopus 로고
    • Quantum Chemistry
    • New York Academic Press.
    • Kauzmann, W. (1957). Quantum Chemistry. New York: Academic Press.
    • (1957)
    • Kauzmann, W.1
  • 112
    • 0002131341 scopus 로고
    • Evidence for conformational and diffusional mean square displacements in frozen aqueous solutions of oxymyoglobin
    • 68–71
    • Keller, H. & Debrunner, P. G. (1980). Evidence for conformational and diffusional mean square displacements in frozen aqueous solutions of oxymyoglobin. Phys. Rev. Lett. 54 (1), 68–71.
    • (1980) Phys. Rev. Lett , vol.54 , Issue.1
    • Keller, H.1    Debrunner, P.G.2
  • 113
    • 0003406737 scopus 로고
    • Solid State Physics
    • 2nd ed. New York: Wiley.
    • Kittel, C. (1956). Solid State Physics, 2nd ed. New York: Wiley.
    • (1956)
    • Kittel, C.1
  • 114
    • 0000988129 scopus 로고
    • Protein dynamics from Moessbauer spectra. The temperature dependence
    • 5042–5047
    • Knapp, E. W., Fischer, S. F. & Parak, F. (1982). Protein dynamics from Moessbauer spectra. The temperature dependence. J. phys. Chem. 86, 5042–5047.
    • (1982) J. phys. Chem , vol.86
    • Knapp, E.W.1    Fischer, S.F.2    Parak, F.3
  • 115
    • 0000108738 scopus 로고
    • The influence of protein dynamics on Moessbauer spectra
    • 4701–4711
    • Knapp, E. W., Fischer, S. F. & Parak, F. (1983). The influence of protein dynamics on Moessbauer spectra. J. chem. Phys. 78 (7), 4701–4711.
    • (1983) J. chem. Phys , vol.78 , Issue.7
    • Knapp, E.W.1    Fischer, S.F.2    Parak, F.3
  • 116
    • 84948502362 scopus 로고
    • Superposition of molecular structures using quaternions
    • (In the Press.)
    • Kneller, G. (1991). Superposition of molecular structures using quaternions. Molecular Simulations. (In the Press.)
    • (1991) Molecular Simulations
    • Kneller, G.1
  • 117
    • 23544450550 scopus 로고
    • Vibrational anomalies are not generally due to fractal geometry: comments on proteins
    • 2696–2699
    • Krumhansl, J. A. (1986). Vibrational anomalies are not generally due to fractal geometry: comments on proteins. Phys. Rev. Lett. 56, 2696–2699.
    • (1986) Phys. Rev. Lett , vol.56
    • Krumhansl, J.A.1
  • 118
    • 0025328145 scopus 로고
    • Temperature dependence of the structure and dynamics of myoglobin. A simulation approach
    • Kuczera, K., Kuriyan, J. & Karplus, M. (1990). Temperature dependence of the structure and dynamics of myoglobin. A simulation approach. J. molec. Biol. 213, 351–373.
    • (1990) J. molec. Biol , vol.213 , pp. 351-373
    • Kuczera, K.1    Kuriyan, J.2    Karplus, M.3
  • 119
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • 239–345
    • Kuntz, I. S. & Kauzmann, W. (1973). Hydration of proteins and polypeptides. Adv. Prot. Chem. 28, 239–345.
    • (1973) Adv. Prot. Chem , vol.28
    • Kuntz, I.S.1    Kauzmann, W.2
  • 120
    • 0023053635 scopus 로고    scopus 로고
    • (1986a). Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation of molecular dynamics. J. molec. Biol. 190, 227—254
    • Kuriyan, J., Petsko, G., Levy, R. M. & Karplus, M. (1986a). Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation of molecular dynamics. J. molec. Biol. 190, 227—254.
    • Kuriyan, J.1    Petsko, G.2    Levy, R.M.3    Karplus, M.4
  • 121
    • 0023042853 scopus 로고    scopus 로고
    • (1986b). X-ray refinement of carbon-monoxy(Fe II)-myoglobin at 1.5 A resolution. J, molec. Biol. 192, 133–154
    • Kuriyan, J., Wilz, S., Karplus, M. & Petsko, G. A. (1986b). X-ray refinement of carbon-monoxy(Fe II)-myoglobin at 1.5 A resolution.J, molec. Biol. 192, 133–154.
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 122
    • 0021762728 scopus 로고    scopus 로고
    • (1984a). Vibrational normal modes of folded prolyl-containing peptides. Application to β turns. Eur. J. Biochem. 139, 149–154
    • Lagant, P., Vergoten, G., Fleury, G. & Loucheux-Lefebvre, M.-H. (1984a). Vibrational normal modes of folded prolyl-containing peptides. Application to β turns. Eur.J. Biochem. 139, 149–154.
    • Lagant, P.1    Vergoten, G.2    Fleury, G.3    Loucheux-Lefebvre, M.-H.4
  • 123
    • 0021762727 scopus 로고    scopus 로고
    • (1984b). Raman spectroscopy and normal vibrations of peptides. Characteristic normal modes of a type II β turn. Eur. J. Biochem. 139, 137–148
    • Lagant, P., Vergoten, G., Fleury, G. & Loucheux-Lefebvre, M.-H. (1984b). Raman spectroscopy and normal vibrations of peptides. Characteristic normal modes of a type II β turn. Eur. J. Biochem. 139, 137–148.
    • Lagant, P.1    Vergoten, G.2    Fleury, G.3    Loucheux-Lefebvre, M.-H.4
  • 124
    • 0000658538 scopus 로고
    • Langevin modes of macromolecules
    • 7334–7348
    • Lamm, G. & Szabo, A. (1986). Langevin modes of macromolecules. J. chem. Phys. 85 (12), 7334–7348.
    • (1986) J. chem. Phys , vol.85 , Issue.12
    • Lamm, G.1    Szabo, A.2
  • 125
    • 0000094594 scopus 로고
    • An iteration method for the solution of the eigenvalue problem of linear differential and integral operators
    • 255–282
    • Lanczos, C. (1950). An iteration method for the solution of the eigenvalue problem of linear differential and integral operators. J. Res. Natl. Bur. Stand. 45, 255–282.
    • (1950) J. Res. Natl. Bur. Stand , vol.45
    • Lanczos, C.1
  • 127
    • 4243857431 scopus 로고
    • Dynamical model of the liquid-glass transition
    • 2765–2773
    • Leutheusser, E. (1984). Dynamical model of the liquid-glass transition. Phys. Rev. A, 29 (5). 2765–2773.
    • (1984) Phys. Rev. A , vol.29 , Issue.5
    • Leutheusser, E.1
  • 128
    • 0022419152 scopus 로고
    • Protein normal mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme
    • 423–447
    • Levitt, M., Sander, C. & Stern, P. S. (1985). Protein normal mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme. J. molec. Biol. 181 (3), 423–447.
    • (1985) J. molec. Biol. 181 , Issue.3
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 129
    • 0024094768 scopus 로고
    • Accurate simulation of protein dynamics in solution
    • 7557–7561
    • Levitt, M. & Sharon, R. (1988). Accurate simulation of protein dynamics in solution. Proc. natn. Acad. Sci. U.S.A. 85, 7557–7561.
    • (1988) Proc. natn. Acad. Sci. U.S.A. 85
    • Levitt, M.1    Sharon, R.2
  • 130
    • 0001200931 scopus 로고    scopus 로고
    • (1981a). Increase of C NMR relaxation times in proteins due to picosecond motional averaging, J. Am. chem. Soc. 103, 994-996
    • Levy, R. M., Karplus, M. & McCammon, J. A. (1981a). Increase of C NMR relaxation times in proteins due to picosecond motional averaging, J. Am. chem. Soc. 103, 994-996.
    • Levy, R.M.1    Karplus, M.2    McCammon, J.A.3
  • 131
    • 0000459946 scopus 로고    scopus 로고
    • (1981b). NMR relaxation parameters in molecules with internal motion: exact Langevin trajectory results compared with simplified relaxation models. J. Am. chem. Soc. 103, 5998–6011
    • Levy, R. M., Karplus, M. & Wolynes, P. G. (1981b). NMR relaxation parameters in molecules with internal motion: exact Langevin trajectory results compared with simplified relaxation models. J. Am. chem. Soc. 103, 5998–6011.
    • Levy, R.M.1    Karplus, M.2    Wolynes, P.G.3
  • 132
    • 0021449809 scopus 로고
    • Quasiharmonic method for studying very low frequency modes in proteins
    • 1099–1112
    • Levy, R. M., Srinivasan, A. R., Olson, W. K. & McCammon, J. A. (1984). Quasiharmonic method for studying very low frequency modes in proteins. Biopolymers 23, 1099–1112.
    • (1984) Biopolymers 23
    • Levy, R.M.1    Srinivasan, A.R.2    Olson, W.K.3    McCammon, J.A.4
  • 133
    • 0242291506 scopus 로고
    • Initial fluoresence depolarisation of tyrosines in proteins
    • 2073–2075
    • Levy, R. M. & Szabo, A. (1982). Initial fluoresence depolarisation of tyrosines in proteins, J. Am. chem. Soc. 104, 2073–2075.
    • (1982) J. Am. chem. Soc , vol.104
    • Levy, R.M.1    Szabo, A.2
  • 135
    • 0019960215 scopus 로고
    • Protein dynamics and NMR relaxation; comparison of simulations with experiment
    • 197–198
    • Lipari, G., Szabo, A. & Levy, R. M. (1982). Protein dynamics and NMR relaxation; comparison of simulations with experiment. Nature, Lond. 300, 197–198.
    • (1982) Nature, Lond. 300
    • Lipari, G.1    Szabo, A.2    Levy, R.M.3
  • 136
    • 0024795316 scopus 로고
    • The effects of truncating long-range forces on protein dynamics
    • 32–45
    • Loncharich, R. J. & Brooks, B. (1989). The effects of truncating long-range forces on protein dynamics. Proteins: Struct. Funct. Genet. 6, 32–45.
    • (1989) Proteins: Struct. Funct. Genet , vol.6
    • Loncharich, R.J.1    Brooks, B.2
  • 137
    • 0025008125 scopus 로고
    • Temperature dependence of dynamics of hydrated myoglobin. Comparison of force field calculations with neutron scattering data
    • 439–455
    • Loncharich, R. J. & Brooks, B. (1990). Temperature dependence of dynamics of hydrated myoglobin. Comparison of force field calculations with neutron scattering data. J. molec. Biol. 215, 439–455.
    • (1990) J. molec. Biol , vol.215
    • Loncharich, R.J.1    Brooks, B.2
  • 138
    • 0003511293 scopus 로고
    • Theory of Neutron Scattering from Condensed Matter
    • International Series of Monographs on Physics, no. 72. Oxford Science Publications. Oxford: Clarendon.
    • Lovesey, S. (1984). Theory of Neutron Scattering from Condensed Matter. International Series of Monographs on Physics, no. 72. Oxford Science Publications. Oxford: Clarendon.
    • (1984)
    • Lovesey, S.1
  • 139
    • 0023431702 scopus 로고
    • Time-resolved fluorescence anisotropy for systems with lifetime and dynamic heterogeneity
    • 59–75
    • Ludescher, R. D., Peting, L., Hudson, S. & Hudson, B. (1987). Time-resolved fluorescence anisotropy for systems with lifetime and dynamic heterogeneity. Biophys. Chem. 28, 59–75.
    • (1987) Biophys. Chem , vol.28
    • Ludescher, R.D.1    Peting, L.2    Hudson, S.3    Hudson, B.4
  • 140
    • 84959634195 scopus 로고
    • Dynamics of Proteins and Nucleic Acids. Cambridge: Cambridge University Press.
    • McCammon, J. A. & Harvey, S. C. (1987). Dynamics of Proteins and Nucleic Acids. Cambridge: Cambridge University Press.
    • (1987)
    • McCammon, J.A.1    Harvey, S.C.2
  • 143
    • 0018798888 scopus 로고
    • Yeast hexokinase in solution exhibits a large conformational change on binding glucose or glucose-6-phosphate
    • 338–342
    • McDonald, R. C., Steitz, T. A. & Engelmann, D. M. (1979). Yeast hexokinase in solution exhibits a large conformational change on binding glucose or glucose-6-phosphate. Biochemistry 18, 338–342.
    • (1979) Biochemistry , vol.18
    • McDonald, R.C.1    Steitz, T.A.2    Engelmann, D.M.3
  • 144
    • 0003527976 scopus 로고
    • Statistical Mechanics
    • New York Harper and Row.
    • McQuarrie, D. (1976). Statistical Mechanics. New York: Harper and Row.
    • (1976)
    • McQuarrie, D.1
  • 145
    • 0001218979 scopus 로고
    • On the infrared and Raman spectra of water in the region 5–200 cm-1
    • 502–506
    • Madden, P. A. & Impey, R. W. (1986). On the infrared and Raman spectra of water in the region 5–200 cm-1. Chem. Phys. Letts. 123 (6), 502–506.
    • (1986) Chem. Phys. Letts , vol.123 , Issue.6
    • Madden, P.A.1    Impey, R.W.2
  • 146
    • 0345203816 scopus 로고
    • Effects of Truncating long range interactions in aqueous ionic solution simulations
    • 105–108
    • Madura, J. & Pettitt, B. M. (1988). Effects of Truncating long range interactions in aqueous ionic solution simulations. Chem. Phys. Lett. 150, 105–108.
    • (1988) Chem. Phys. Lett. 150
    • Madura, J.1    Pettitt, B.M.2
  • 147
    • 84950746455 scopus 로고
    • Neutron Facilities at the ILL High Flux Reactor. Grenoble
    • Institut Laue-Langevin
    • Maier, B. (1983). Neutron Facilities at the ILL High Flux Reactor. Grenoble: Institut Laue-Langevin.
    • (1983)
    • Maier, B.1
  • 148
    • 0020200488 scopus 로고
    • Molecular dynamics of ferrocytochrome C: anharmonicity of atomic displacements
    • 1979–1989
    • Mao, B., Pear, M. R., McCammon, J. A. & Northrup, S. H. (1982). Molecular dynamics of ferrocytochrome C: anharmonicity of atomic displacements. Biopolymers 21, 1979–1989.
    • (1982) Biopolymers , vol.21
    • Mao, B.1    Pear, M.R.2    McCammon, J.A.3    Northrup, S.H.4
  • 149
    • 0020825723 scopus 로고
    • Structural dynamics of human deoxyhemoglobin and hemochrome investigated by nuclear gamma resonance absorption (Moessbauer) spectroscopy
    • 5294–5296
    • Mayo, K. H., Kucheida, D., Parak, F. & Chien, J. C. W. (1983). Structural dynamics of human deoxyhemoglobin and hemochrome investigated by nuclear gamma resonance absorption (Moessbauer) spectroscopy. Proc. natn. Acad. Sci. U.S.A. 80, 5294–5296.
    • (1983) Proc. natn. Acad. Sci. U.S.A , vol.80
    • Mayo, K.H.1    Kucheida, D.2    Parak, F.3    Chien, J.C.W.4
  • 150
    • 0001556207 scopus 로고
    • Observations of elastic and quasielastic nuclear gamma resonance absorption in hemoglobin crystals
    • 82 A, 468–470
    • Mayo, K. H., Parak, F. & Moessbauer, R. L. (1981). Observations of elastic and quasielastic nuclear gamma resonance absorption in hemoglobin crystals. Phys. Lett. 82 A, 468–470.
    • (1981) Phys. Lett
    • Mayo, K.H.1    Parak, F.2    Moessbauer, R.L.3
  • 151
    • 0021192461 scopus 로고
    • Biophysical applications of quasi elastic and inelastic neutron scattering
    • 425–451
    • Middendorf, H. D. (1984). Biophysical applications of quasi elastic and inelastic neutron scattering. Rev. Biophys. Bioengng. 13, 425–451.
    • (1984) Rev. Biophys. Bioengng , vol.13
    • Middendorf, H.D.1
  • 152
    • 84959581788 scopus 로고
    • Neutron spectroscopy and protein dynamics
    • Structure and Motion; Membranes, Nucleic Acids and Proteins (ed. E. Clementi and R. H. Sarma). Adenine Press
    • Middendorf, H. D. & Randall, J. T. (1985). Neutron spectroscopy and protein dynamics. In Structure and Motion; Membranes, Nucleic Acids and Proteins (ed. E. Clementi and R. H. Sarma). Adenine Press.
    • (1985)
    • Middendorf, H.D.1    Randall, J.T.2
  • 153
    • 46149135975 scopus 로고
    • A next generation steady state neutron source
    • 137 B, 347–358
    • Moon, R. M. & West, C. D. (1986). A next generation steady state neutron source. Physica 137 B, 347–358.
    • (1986) Physica
    • Moon, R.M.1    West, C.D.2
  • 154
    • 0024301735 scopus 로고
    • The advanced neutron source
    • 156 and 157, 522–524
    • Moon, R. M. & West, C. D. (1989). The advanced neutron source. Physica 156 and 157, 522–524.
    • (1989) Physica
    • Moon, R.M.1    West, C.D.2
  • 155
    • 35949023042 scopus 로고
    • Temperature-dependence of the dynamic structure factor and the stability of a supercooled liquid: a molecular dynamics study of liquid rubidium
    • A 28, 370–372
    • Mountain, R. D. & Basu, P. K. (1983). Temperature-dependence of the dynamic structure factor and the stability of a supercooled liquid: a molecular dynamics study of liquid rubidium. Phys. Rev. A 28, 370–372.
    • (1983) Phys. Rev
    • Mountain, R.D.1    Basu, P.K.2
  • 156
    • 0018337803 scopus 로고
    • Subnanosecond motions of tryptophan residues in proteins
    • 56–60
    • Munro, I., Pecht, I. & Stryer, L. (1979). Subnanosecond motions of tryptophan residues in proteins. Proc. natn. Acad. Sci. U.S.A. 76, 56–60.
    • (1979) Proc. natn. Acad. Sci. U.S.A , vol.76
    • Munro, I.1    Pecht, I.2    Stryer, L.3
  • 157
    • 6044276402 scopus 로고
    • Inelastic neutron scattering study of the torsional and CCC bend frequencies in the solid n-alkanes, ethane-hexane
    • 2447–2454
    • Nelligan, W. B., Lepoire, D. J., Brun, T. O. & Kleb, R. (1987). Inelastic neutron scattering study of the torsional and CCC bend frequencies in the solid n-alkanes, ethane-hexane. J. chem. Phys. 87 (5), 2447–2454.
    • (1987) J. chem. Phys , vol.87 , Issue.5
    • Nelligan, W.B.1    Lepoire, D.J.2    Brun, T.O.3    Kleb, R.4
  • 158
    • 34748868767 scopus 로고
    • Protein crystal dynamics studied by time resolved analysis of X-ray diffuse scattering
    • 665–666
    • Nienhaus, G., Heinzl, J., Huenges, E. & Parak, F. (1989). Protein crystal dynamics studied by time resolved analysis of X-ray diffuse scattering. Nature, Lond. 338, 665–666.
    • (1989) Nature, Lond , vol.338
    • Nienhaus, G.1    Heinzl, J.2    Huenges, E.3    Parak, F.4
  • 159
    • 33744715201 scopus 로고
    • Time expansion of correlation functions and the theory of slow neutron scattering
    • 415–432
    • Nijboer, B. R. A. & Rahman, A. (1966). Time expansion of correlation functions and the theory of slow neutron scattering. Physica 32, 415–432.
    • (1966) Physica , vol.32
    • Nijboer, B.R.A.1    Rahman, A.2
  • 160
    • 0023613529 scopus 로고
    • Normal modes of vibration in bovine pancreatic trypsin inhibitor and its mechanical property
    • 308–329
    • Nishikawa, T. & Go, N. (1987). Normal modes of vibration in bovine pancreatic trypsin inhibitor and its mechanical property. Proteins: Struct. Funct. Genet. 2, 308–329.
    • (1987) Proteins: Struct. Funct. Genet , vol.2
    • Nishikawa, T.1    Go, N.2
  • 161
    • 0020813608 scopus 로고
    • Dynamics of globular proteins in terms of dihedral angles
    • 3283–3288
    • Noguti, T. & Go, N. (1983). Dynamics of globular proteins in terms of dihedral angles. J. Phys. Soc. Jap. 52, 3283–3288.
    • (1983) J. Phys. Soc. Jap , pp. 52
    • Noguti, T.1    Go, N.2
  • 162
    • 0024585391 scopus 로고    scopus 로고
    • (1989a). Structural basis of hierarchical multiple substates of a protein. I. Introduction. Proteins: Struct. Funct. Genet. 5, 97–103
    • Noguti, T. & Go, N. (1989a). Structural basis of hierarchical multiple substates of a protein. I. Introduction. Proteins: Struct. Funct. Genet. 5, 97–103.
    • Noguti, T.1    Go, N.2
  • 163
    • 0024567779 scopus 로고    scopus 로고
    • (1989b). Structural basis of hierarchical multiple substates of a protein. II. Monte Carlo simulation of native thermal fluctuations and energy minimisation. Proteins: Struct. Funct. Genet. 5, 104–112
    • Noguti, T. & Go, N. (1989b). Structural basis of hierarchical multiple substates of a protein. II. Monte Carlo simulation of native thermal fluctuations and energy minimisation. Proteins: Struct. Funct. Genet. 5, 104–112.
    • Noguti, T.1    Go, N.2
  • 164
    • 0024486487 scopus 로고    scopus 로고
    • (1989c). Structural basis of hierarchical multiple substates of protein. III. Side chain and main chain local conformations. Proteins: Struct. Funct. Genet. 5, 113–124
    • Noguti, T. & Go, N. (1989c). Structural basis of hierarchical multiple substates of protein. III. Side chain and main chain local conformations. Proteins: Struct. Funct. Genet. 5, 113–124.
    • Noguti, T.1    Go, N.2
  • 165
    • 0024486623 scopus 로고    scopus 로고
    • (1989d). Structural basis of hierarchical multiple substates of a protein. IV. Rearrangements in atom packing and local deformations. Proteins: Struct. Funct. Genet. 5, 125–131
    • Noguti, T. & Go, N. (1989d). Structural basis of hierarchical multiple substates of a protein. IV. Rearrangements in atom packing and local deformations. Proteins: Struct. Funct. Genet. 5, 125–131.
    • Noguti, T.1    Go, N.2
  • 166
    • 0024486201 scopus 로고    scopus 로고
    • (1989e). Structural basis of hierarchical multiple substates of a protein. V. Nonlocal deformations. Proteins: Struct. Funct. Genet. 5, 132–138
    • Noguti, T. & Go, N. (1989e). Structural basis of hierarchical multiple substates of a protein. V. Nonlocal deformations. Proteins: Struct. Funct. Genet. 5, 132–138.
    • Noguti, T.1    Go, N.2
  • 167
    • 0542362994 scopus 로고
    • Rate theory for gated diffusion-influenced ligand binding to proteins
    • 2314–2321
    • Northrup, S. H., Zarrin, F. & McCammon, J. A. (1982). Rate theory for gated diffusion-influenced ligand binding to proteins. J. phys. Chem. 86, 2314–2321.
    • (1982) J. phys. Chem , vol.86
    • Northrup, S.H.1    Zarrin, F.2    McCammon, J.A.3
  • 168
    • 0000633398 scopus 로고
    • Spectral shapes of Moessbauer absorption and incoherent neutron scattering from harmonically bound nuclei in Brownian motion: application to macromolecular systems
    • 2291–2299
    • Nowik, I., Bauminger, E. R., Cohen, S. G. & Ofer, S. (1985). Spectral shapes of Moessbauer absorption and incoherent neutron scattering from harmonically bound nuclei in Brownian motion: application to macromolecular systems. Phys. Rev. A 31 (4), 2291–2299.
    • (1985) Phys. Rev. A 31 , Issue.4
    • Nowik, I.1    Bauminger, E.R.2    Cohen, S.G.3    Ofer, S.4
  • 169
    • 0022667455 scopus 로고
    • Dynamics of fractal networks
    • 814–819
    • Orbach, R. (1986). Dynamics of fractal networks. Science, Wash. 231, 814–819.
    • (1986) Science, Wash , vol.231
    • Orbach, R.1
  • 170
    • 0022548205 scopus 로고
    • Water molecule dynamics in hydrated lysozyme. A deuteron magnetic resonance study
    • 943–948
    • Peemoeller, H., Yeomans, F. G., Kydon, D. W. & Sharp, A. R. (1986). Water molecule dynamics in hydrated lysozyme. A deuteron magnetic resonance study. Biophys. J. 49, 943–948.
    • (1986) Biophys. J , vol.49
    • Peemoeller, H.1    Yeomans, F.G.2    Kydon, D.W.3    Sharp, A.R.4
  • 171
    • 0018371101 scopus 로고
    • Low frequency vibrations and the dynamics of proteins and peptides
    • 425–458
    • Peticolas, W. (1979). Low frequency vibrations and the dynamics of proteins and peptides. Meth. Enzymol. 61, 425–458.
    • (1979) Meth. Enzymol , vol.61
    • Peticolas, W.1
  • 172
    • 0018606116 scopus 로고
    • Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase
    • 11323–11329
    • Pickover, C. A., McKay, D. B., Engelman, D. M. & Steitz, T. A. (1979). Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. J. biol. Chem. 254, 11323–11329.
    • (1979) J. biol. Chem , vol.254
    • Pickover, C.A.1    McKay, D.B.2    Engelman, D.M.3    Steitz, T.A.4
  • 173
    • 0021762782 scopus 로고
    • Picosecond relaxations in hydrated lysozyme observed by mm-wave spectroscopy
    • 137–142
    • Poglitsch, A., Kremer, F. & Genzel, L. (1984). Picosecond relaxations in hydrated lysozyme observed by mm-wave spectroscopy. J. molec. Biol. 173, 137–142.
    • (1984) J. molec. Biol , vol.173
    • Poglitsch, A.1    Kremer, F.2    Genzel, L.3
  • 174
    • 0024406542 scopus 로고
    • A molecular dynamics analysis of protein structural elements
    • 337–354
    • Post, C. B., Dobson, C. M. & Karplus, M. (1989). A molecular dynamics analysis of protein structural elements. Proteins: Struct. Funct. Genet. 5, 337–354.
    • (1989) Proteins: Struct. Funct. Genet , vol.5
    • Post, C.B.1    Dobson, C.M.2    Karplus, M.3
  • 175
    • 33846611337 scopus 로고
    • Hydration-induced conformational and flexibility changes in lysozyme at low water content
    • 308—310
    • Poole, P. L. & Finney, J. L. (1983). Hydration-induced conformational and flexibility changes in lysozyme at low water content. Int. J. Biol. Macromolecules 5, 308—310.
    • (1983) Int. J. Biol. Macromolecules 5
    • Poole, P.L.1    Finney, J.L.2
  • 176
    • 24344441402 scopus 로고
    • Low frequency intermolecular modes in deuterated α-glycine
    • 165–167
    • Powell, B. M. & Martel, P. (1979). Low frequency intermolecular modes in deuterated α-glycine. Chem. Phys. Lett. 67, 165–167.
    • (1979) Chem. Phys. Lett , vol.67
    • Powell, B.M.1    Martel, P.2
  • 177
    • 0019485043 scopus 로고
    • Hydrogen bonding in DNA base complexes
    • 311–323
    • Powell, B. M. & Martel, P. (1981). Hydrogen bonding in DNA base complexes. Biophys. J. 34, 311–323.
    • (1981) Biophys. J , vol.34
    • Powell, B.M.1    Martel, P.2
  • 178
    • 0008624423 scopus 로고
    • Intermediate scattering function in slow neutron scattering
    • 1334–1346
    • Rahman, A. (1963). Intermediate scattering function in slow neutron scattering. Phys. Rev. 130 (4), 1334–1346.
    • (1963) Phys. Rev , vol.130 , Issue.4
    • Rahman, A.1
  • 179
    • 36149006945 scopus 로고    scopus 로고
    • (1962a). Theory of slow neutron scattering by liquids. I. Phys. Rev. 126, 986–996
    • Rahman, A., Singwi, K. S. & Sjolander, A. (1962a). Theory of slow neutron scattering by liquids. I. Phys. Rev. 126, 986–996.
    • Rahman, A.1    Singwi, K.S.2    Sjolander, A.3
  • 180
    • 0342773497 scopus 로고    scopus 로고
    • (1962b). Stochastic model of a liquid and cold neutron scattering. II. Phys. Rev. 126, 997–1004
    • Rahman, A., Singwi, K. S. & Sjolander, A. (1962b). Stochastic model of a liquid and cold neutron scattering. II. Phys. Rev. 126, 997–1004.
    • Rahman, A.1    Singwi, K.S.2    Sjolander, A.3
  • 181
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution
    • III-152
    • Remington, S., Wiegand, G. & Huber, R. (1982). Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. J. molec. Biol. 158, III-152.
    • (1982) J. molec. Biol , vol.158
    • Remington, S.1    Wiegand, G.2    Huber, R.3
  • 182
    • 4244123276 scopus 로고
    • Collective relaxation of star polymers-A neutron spin-echo study
    • 2462–2465
    • Richter, D., Stuhn, B., Ewen, B. & Nerger, D. (1987). Collective relaxation of star polymers-A neutron spin-echo study. Phys. Rev. Lett. 58 (23), 2462–2465.
    • (1987) Phys. Rev. Lett , vol.58 , Issue.23
    • Richter, D.1    Stuhn, B.2    Ewen, B.3    Nerger, D.4


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