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Volumn 91, Issue 7, 2006, Pages 2573-2588

Influence of hydration on the dynamics of lysozyme

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME;

EID: 33749487679     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.082214     Document Type: Article
Times cited : (204)

References (78)
  • 3
    • 0001098010 scopus 로고    scopus 로고
    • The dynamical transition in proteins: The role of hydrogen bonds
    • M. C. Bellissent-Funel, editor. IOS Press, Les Houches, France
    • Doster, W., and M. Settles. 1998. The dynamical transition in proteins: the role of hydrogen bonds. In Workshop on Hydration Processes in Biology: Theoretical and Experimental Approaches. M. C. Bellissent-Funel, editor. IOS Press, Les Houches, France. 177-191.
    • (1998) Workshop on Hydration Processes in Biology: Theoretical and Experimental Approaches , pp. 177-191
    • Doster, W.1    Settles, M.2
  • 5
    • 0025877453 scopus 로고
    • Protein hydration and function
    • Rupley, J. A., and G. Careri. 1991. Protein hydration and function. Adv. Protein Chem. 41:37-172.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 6
    • 0037292622 scopus 로고    scopus 로고
    • Physical aspects of protein dynamics
    • Parak, F. G. 2003. Physical aspects of protein dynamics. Rep. Prog. Phys. 66:103-129.
    • (2003) Rep. Prog. Phys. , vol.66 , pp. 103-129
    • Parak, F.G.1
  • 7
    • 0043194670 scopus 로고    scopus 로고
    • Evolution of the internal dynamics of two globular proteins from dry powder to solution
    • Perez, J., J. M. Zanotti, and D. Durand. 1999. Evolution of the internal dynamics of two globular proteins from dry powder to solution. Biophys. J. 77:454-469.
    • (1999) Biophys. J. , vol.77 , pp. 454-469
    • Perez, J.1    Zanotti, J.M.2    Durand, D.3
  • 8
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • Doster, W., S. Cusack, and W. Petry. 1989. Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature. 337:754-756.
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 9
    • 0030823236 scopus 로고    scopus 로고
    • Picosecond molecular motions in bacteriorhodopsin from neutron scattering
    • Fitter, J., R. E. Lechner, and N. A. Dencher. 1997. Picosecond molecular motions in bacteriorhodopsin from neutron scattering. Biophys. J. 73:2126-2137.
    • (1997) Biophys. J. , vol.73 , pp. 2126-2137
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 10
    • 0030862281 scopus 로고    scopus 로고
    • Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering
    • Diehl, M., W. Doster, W. Petry, and H. Schober. 1997. Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering. Biophys. J. 73:2726-2732.
    • (1997) Biophys. J. , vol.73 , pp. 2726-2732
    • Diehl, M.1    Doster, W.2    Petry, W.3    Schober, H.4
  • 11
    • 0033747018 scopus 로고    scopus 로고
    • Molecular dynamics of solid-state lysozyme as affected by glycerol and water: A neutron scattering study
    • Tsai, A. M., D. A. Neumann, and L. N. Bell. 2000. Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study. Biophys. J. 79:2728-2732.
    • (2000) Biophys. J. , vol.79 , pp. 2728-2732
    • Tsai, A.M.1    Neumann, D.A.2    Bell, L.N.3
  • 13
    • 0031548675 scopus 로고    scopus 로고
    • Dynamics of a globular protein studied by neutron scattering and solid-state NMR
    • Zanotti, J. M., M. C. Bellissent-Funel, and J. Parello. 1997. Dynamics of a globular protein studied by neutron scattering and solid-state NMR. Physica B (Amsterdam). 234-236:228-230.
    • (1997) Physica B (Amsterdam) , vol.234-236 , pp. 228-230
    • Zanotti, J.M.1    Bellissent-Funel, M.C.2    Parello, J.3
  • 14
    • 0026720247 scopus 로고
    • Crystalline ribonuclease a losese function below the dynamical transition at 200 K
    • Rasmussen, B. F., A. M. Stock, D. Ringe, and G. A. Petsko. 1992. Crystalline ribonuclease A losese function below the dynamical transition at 200 K. Nature. 357:423-424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 15
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the environment on the protein dynamical transition: A neutron scattering study
    • Paciaroni, A., S. Cinelli, and G. Onori. 2002. Effect of the environment on the protein dynamical transition: a neutron scattering study. Biophys. J. 83:1157-1164.
    • (2002) Biophys. J. , vol.83 , pp. 1157-1164
    • Paciaroni, A.1    Cinelli, S.2    Onori, G.3
  • 17
    • 0000464216 scopus 로고
    • A consistent picture of protein dynamics
    • Parak, F., and E. W. Knapp. 1984. A consistent picture of protein dynamics. Proc. Natl. Acad. Sci. USA. 81:7088-7092.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7088-7092
    • Parak, F.1    Knapp, E.W.2
  • 18
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membrane: Effects of temperature and hydration studied by neutron scattering
    • Ferrand, M., A. J. Dianoux, W. Petry, and G. Zaccai. 1993. Thermal motions and function of bacteriorhodopsin in purple membrane: effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA. 90:9668-9672.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 19
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • Ostermann, A., R. Waschipky, F. G. Parak, and G. U. Nienhaus. 2000. Ligand binding and conformational motions in myoglobin. Nature. 404:205-208.
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak, F.G.3    Nienhaus, G.U.4
  • 21
    • 0033064923 scopus 로고    scopus 로고
    • The temperature dependence of internal molecular motions in hydrated and dry a-amylase: The role of hydration water in the dynamical transition of proteins
    • Fitter, J. 1999. The temperature dependence of internal molecular motions in hydrated and dry a-amylase: the role of hydration water in the dynamical transition of proteins. Biophys. J. 76:1034-1042.
    • (1999) Biophys. J. , vol.76 , pp. 1034-1042
    • Fitter, J.1
  • 23
    • 0032574827 scopus 로고    scopus 로고
    • Dynamics and function of proteins: The search for general concepts
    • Frauenfelder, H., and B. McMahon. 1998. Dynamics and function of proteins: the search for general concepts. Proc. Natl. Acad. Sci. USA. 95:4795-4797.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4795-4797
    • Frauenfelder, H.1    McMahon, B.2
  • 24
    • 0042861647 scopus 로고    scopus 로고
    • Translational hydration water dynamics drives the protein glass transition
    • Tournier, A. L., J. Xu, and J. C. Smith. 2003. Translational hydration water dynamics drives the protein glass transition. Biophys. J. 85:1871-1875.
    • (2003) Biophys. J. , vol.85 , pp. 1871-1875
    • Tournier, A.L.1    Xu, J.2    Smith, J.C.3
  • 25
    • 0346216028 scopus 로고    scopus 로고
    • Principal components of the protein dynamical transition
    • Tournier, A. L., and J. C. Smith. 2003. Principal components of the protein dynamical transition. Phys. Rev. Lett. 91:208106.
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 208106
    • Tournier, A.L.1    Smith, J.C.2
  • 27
    • 0034163362 scopus 로고    scopus 로고
    • Enzyme activity and dynamics: Xylanase activity in the absence of fast anharmonic dynamics
    • Dunn, R. V., V. Réat, J. Finney, M. Ferrand, J. C. Smith, and R. M. Daniel. 2000. Enzyme activity and dynamics: xylanase activity in the absence of fast anharmonic dynamics. Biochem. J. 346:355-358.
    • (2000) Biochem. J. , vol.346 , pp. 355-358
    • Dunn, R.V.1    Réat, V.2    Finney, J.3    Ferrand, M.4    Smith, J.C.5    Daniel, R.M.6
  • 29
    • 19044399611 scopus 로고    scopus 로고
    • Role of protein-water hydrogen bond dynamics in the protein dynamical transition
    • Tarek, M., and D. J. Tobias. 2002. Role of protein-water hydrogen bond dynamics in the protein dynamical transition. Phys. Rev. Lett. 88:138101.
    • (2002) Phys. Rev. Lett. , vol.88 , pp. 138101
    • Tarek, M.1    Tobias, D.J.2
  • 30
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? A protein dynamics force constant measured by neutron scattering
    • Zaccai, G. 2000. How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science. 288:1604-1607.
    • (2000) Science , vol.288 , pp. 1604-1607
    • Zaccai, G.1
  • 32
    • 0028100759 scopus 로고
    • Liquid-like side-chain dynamics in myoglobin
    • Kneller, G. R., and J. C. Smith. 1994. Liquid-like side-chain dynamics in myoglobin. J. Mol. Biol. 242:181-185.
    • (1994) J. Mol. Biol. , vol.242 , pp. 181-185
    • Kneller, G.R.1    Smith, J.C.2
  • 33
    • 0022020855 scopus 로고
    • Hydrogen-exchange evidence for distinct structural classes in globular proteins
    • Gregory, R. B., and R. W. Lumry. 1985. Hydrogen-exchange evidence for distinct structural classes in globular proteins. Biopolymers. 24:301-326.
    • (1985) Biopolymers , vol.24 , pp. 301-326
    • Gregory, R.B.1    Lumry, R.W.2
  • 34
    • 0033613906 scopus 로고    scopus 로고
    • Native proteins are surface-molten solids: Application of the Lindemann criterion for the solid versus liquid state
    • Zhou, Y., D. Vitkup, and M. J. Karplus. 1999. Native proteins are surface-molten solids: application of the Lindemann criterion for the solid versus liquid state. J. Mol. Biol. 285:1371-1375.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1371-1375
    • Zhou, Y.1    Vitkup, D.2    Karplus, M.J.3
  • 35
    • 0036722914 scopus 로고    scopus 로고
    • Dynamic transition in lysozyme: Role of a solvent
    • Caliskan, G., A. Kisliuk, and A. P. Sokolov. 2002. Dynamic transition in lysozyme: role of a solvent. J. Non-Cryst. Sol. 307-310:868-873.
    • (2002) J. Non-Cryst. Sol. , vol.307-310 , pp. 868-873
    • Caliskan, G.1    Kisliuk, A.2    Sokolov, A.P.3
  • 36
    • 0022425369 scopus 로고
    • Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions
    • Schinkel, J. E., N. W. Downer, and J. A. Rupley. 1984. Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions. Biochemistry. 24:352-366.
    • (1984) Biochemistry , vol.24 , pp. 352-366
    • Schinkel, J.E.1    Downer, N.W.2    Rupley, J.A.3
  • 37
    • 10844239741 scopus 로고    scopus 로고
    • Lysozyme-water interactions studied by sorption calorimetry
    • Kocherbitov, V., T. Arnebrant, and O. Söderman. 2004. Lysozyme-water interactions studied by sorption calorimetry. J. Phys. Chem. B. 108:19036-19042.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 19036-19042
    • Kocherbitov, V.1    Arnebrant, T.2    Söderman, O.3
  • 40
    • 85030601837 scopus 로고    scopus 로고
    • NIST. 2005. http://www.ncnr.nist.gov/dave
    • (2005)
  • 41
    • 0015994218 scopus 로고
    • Real-space refinement of the structure of hen egg-white lysozyme
    • Diamond, R. 1974. Real-space refinement of the structure of hen egg-white lysozyme. J. Mol. Biol. 82:371-391.
    • (1974) J. Mol. Biol. , vol.82 , pp. 371-391
    • Diamond, R.1
  • 42
    • 51149211502 scopus 로고
    • Improved simulation of liquid water by molecular dynamics
    • Stillinger, F. H., and A. Rahman. 1974. Improved simulation of liquid water by molecular dynamics. J. Chem. Phys. 60:1545-1557.
    • (1974) J. Chem. Phys. , vol.60 , pp. 1545-1557
    • Stillinger, F.H.1    Rahman, A.2
  • 45
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 46
    • 0034715463 scopus 로고    scopus 로고
    • Amplitudes and frequencies of protein dynamics: Analysis of discrepancies between neutron scattering and molecular dynamics simulations
    • Tarek, M., G. J. Martyna, and D. J. Tobias. 2000. Amplitudes and frequencies of protein dynamics: analysis of discrepancies between neutron scattering and molecular dynamics simulations. J. Am. Chem. Soc. 122:10450-10451.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10450-10451
    • Tarek, M.1    Martyna, G.J.2    Tobias, D.J.3
  • 49
    • 0344863187 scopus 로고    scopus 로고
    • Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: Correlation with kinetics and light-induced conformational changes
    • Lehnert, U., V. Réat, M. Weik, G. Zaccai, and C. Pfister. 1998. Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes. Biophys. J. 75:1945-1952.
    • (1998) Biophys. J. , vol.75 , pp. 1945-1952
    • Lehnert, U.1    Réat, V.2    Weik, M.3    Zaccai, G.4    Pfister, C.5
  • 50
    • 0035118232 scopus 로고    scopus 로고
    • Protein flexibility from dynamical transition: A force constant analysis
    • Bicout, D. J., and G. Zaccai. 2001. Protein flexibility from dynamical transition: a force constant analysis. Biophys. J. 80:1115-1123.
    • (2001) Biophys. J. , vol.80 , pp. 1115-1123
    • Bicout, D.J.1    Zaccai, G.2
  • 51
    • 0001706226 scopus 로고
    • Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering
    • Doster, W., S. Cusack, and W. Petry. 1990. Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering. Phys. Rev. Lett. 65:1080-1084.
    • (1990) Phys. Rev. Lett. , vol.65 , pp. 1080-1084
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 52
    • 0000409076 scopus 로고    scopus 로고
    • Glassy dynamics in DNA: Ruled by water of hydration?
    • Sokolov, A. P., H. Grimm, and R. Kahn. 1999. Glassy dynamics in DNA: ruled by water of hydration? J. Chem. Phys. 110:7053-7057.
    • (1999) J. Chem. Phys. , vol.110 , pp. 7053-7057
    • Sokolov, A.P.1    Grimm, H.2    Kahn, R.3
  • 53
    • 0030927638 scopus 로고    scopus 로고
    • Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering
    • Veronique, R., P. Calmettes, J. C. Smith, M. Desmadril, G. Goddens, and D. Durand. 1997. Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering. Proteins. 28:380-387.
    • (1997) Proteins , vol.28 , pp. 380-387
    • Veronique, R.1    Calmettes, P.2    Smith, J.C.3    Desmadril, M.4    Goddens, G.5    Durand, D.6
  • 54
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    • Cordone, L., M. Ferrand, E. Vitrano, and G. Zaccai. 1999. Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biophys. J. 76:1043-1047.
    • (1999) Biophys. J. , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 55
    • 0036193327 scopus 로고    scopus 로고
    • Temperature dependence of protein dynamics: Computer simulation analysis of neutron scattering properties
    • Hayward, J. A., and J. C. Smith. 2002. Temperature dependence of protein dynamics: computer simulation analysis of neutron scattering properties. Biophys. J. 82:1216-1225.
    • (2002) Biophys. J. , vol.82 , pp. 1216-1225
    • Hayward, J.A.1    Smith, J.C.2
  • 56
    • 0001026117 scopus 로고
    • Proton magnetic relaxation of proteins in the solid state: Molecular dynamics of ribonuclease
    • Andrew, E. R., D. J. Bryant, and E. M. Cashell. 1980. Proton magnetic relaxation of proteins in the solid state: molecular dynamics of ribonuclease. Chem. Phys. Lett. 69:551-554.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 551-554
    • Andrew, E.R.1    Bryant, D.J.2    Cashell, E.M.3
  • 57
    • 0021765655 scopus 로고
    • Nuclear magnetic resonance studies of amino acids and proteins. Deuterium nuclear magnetic resonance relaxation of deuteriomethyl-labeled amino acids in crystals and in halobacterium halobium and Escherichia coli cell membranes
    • Keniry, M. A., A. Kintanar, R. L. Smith, H. S. Gutowsky, and E. Oldfield. 1984. Nuclear magnetic resonance studies of amino acids and proteins. Deuterium nuclear magnetic resonance relaxation of deuteriomethyl-labeled amino acids in crystals and in halobacterium halobium and Escherichia coli cell membranes. Biochemistry. 23:288-298.
    • (1984) Biochemistry , vol.23 , pp. 288-298
    • Keniry, M.A.1    Kintanar, A.2    Smith, R.L.3    Gutowsky, H.S.4    Oldfield, E.5
  • 59
    • 0029836757 scopus 로고    scopus 로고
    • Internal molecular motions of bacteriorhodopsin: Hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes
    • Fitter, J., R. E. Lechner, G. Büldt, and N. A. Dencher. 1996. Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes. Proc. Natl. Acad. Sci. USA. 93:7600-7605.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7600-7605
    • Fitter, J.1    Lechner, R.E.2    Büldt, G.3    Dencher, N.A.4
  • 60
    • 20144366574 scopus 로고    scopus 로고
    • Protein-water displacement distributions
    • Doster, W., and M. Settles. 2005. Protein-water displacement distributions. Biochim. Biophys. Acta 1749:173-186.
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 173-186
    • Doster, W.1    Settles, M.2
  • 61
    • 85030603567 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 62
    • 0028378785 scopus 로고
    • Methyl group dynamics in glassy polyisoprene: A neutron backscattering investigation
    • Frick, B., and L. J. Fetters. 1994. Methyl group dynamics in glassy polyisoprene: a neutron backscattering investigation. Macromolecules. 27:974-980.
    • (1994) Macromolecules , vol.27 , pp. 974-980
    • Frick, B.1    Fetters, L.J.2
  • 63
    • 0001344515 scopus 로고
    • Proton magnetic relaxation and molecular motion in polycrystalline amino acids I. Aspartic acid, cystine, glycine, histidine, serine, tryptophan and tyrosine
    • Andrew, E. R., W. S. Hinshaw, M. G. Hutchins, and R. O. I. Sjöblom. 1976. Proton magnetic relaxation and molecular motion in polycrystalline amino acids I. Aspartic acid, cystine, glycine, histidine, serine, tryptophan and tyrosine. Mol. Phys. 31:1479-1488.
    • (1976) Mol. Phys. , vol.31 , pp. 1479-1488
    • Andrew, E.R.1    Hinshaw, W.S.2    Hutchins, M.G.3    Sjöblom, R.O.I.4
  • 64
    • 0011309059 scopus 로고
    • Proton magnetic relaxation and molecular motion in polycrystalline amino acids II. Alanine, isoleucine, leucine, methionine, norleucine, threonine and valine
    • Andrew, E. R., W. S. Hinshaw, M. G. Hutchins, R. O. I. Sjöblom, and P. C. Canepa. 1976. Proton magnetic relaxation and molecular motion in polycrystalline amino acids II. Alanine, isoleucine, leucine, methionine, norleucine, threonine and valine. Mol. Phys. 32:795-806.
    • (1976) Mol. Phys. , vol.32 , pp. 795-806
    • Andrew, E.R.1    Hinshaw, W.S.2    Hutchins, M.G.3    Sjöblom, R.O.I.4    Canepa, P.C.5
  • 65
    • 84947392487 scopus 로고
    • Proton magnetic relaxation and molecular motion in polycrystalline amino acids III. Arginine, asparagines, cysteine, glutamine, phenylalanine and proline
    • Andrew, E. R., W. S. Hinshaw, M. G. Hutchins, and R. O. I. Sjöblom. 1977. Proton magnetic relaxation and molecular motion in polycrystalline amino acids III. Arginine, asparagines, cysteine, glutamine, phenylalanine and proline. Mol. Phys. 34:1695-1706.
    • (1977) Mol. Phys. , vol.34 , pp. 1695-1706
    • Andrew, E.R.1    Hinshaw, W.S.2    Hutchins, M.G.3    Sjöblom, R.O.I.4
  • 67
    • 0018570657 scopus 로고
    • X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme
    • Kelly, J. A., A. R. Sielecki, B. D. Sykes, M. N. G. James, and D. C. Phillips. 1979. X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme. Nature. 282:875-878.
    • (1979) Nature , vol.282 , pp. 875-878
    • Kelly, J.A.1    Sielecki, A.R.2    Sykes, B.D.3    James, M.N.G.4    Phillips, D.C.5
  • 68
    • 0022111715 scopus 로고
    • Normal modes for specific motions of macromolecules: Application to the hinge-bending mode of lysozyme
    • Brooks, B., and M. Karplus. 1985. Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme. Proc. Natl. Acad. Sci. USA. 82:4995-4999.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4995-4999
    • Brooks, B.1    Karplus, M.2
  • 70
    • 0008359643 scopus 로고    scopus 로고
    • On the origin of the non-exponential behavior of the a-relaxation in glass-forming polymers: Incoherent neutron scattering and dielectric relaxation results
    • Colmenero, J., A. Arbe, A. Alegría, M. Monkenbusch, and D. Richter. 1999. On the origin of the non-exponential behavior of the a-relaxation in glass-forming polymers: incoherent neutron scattering and dielectric relaxation results. J. Phys. Condens. Matter. 11:A363-A370.
    • (1999) J. Phys. Condens. Matter. , vol.11
    • Colmenero, J.1    Arbe, A.2    Alegría, A.3    Monkenbusch, M.4    Richter, D.5
  • 71
    • 0035811318 scopus 로고    scopus 로고
    • Correlations of the boson peak with positron annihilation in series of polycarbonate copolymers
    • Soles, C., R. M. Dimeo, D. A. Neumann, A. Kisliuk, A. P. Sokolov, J. Liu, A. F. Yee, and W. L. Wu. 2001. Correlations of the boson peak with positron annihilation in series of polycarbonate copolymers. Macromolecules. 34:4082-4088.
    • (2001) Macromolecules , vol.34 , pp. 4082-4088
    • Soles, C.1    Dimeo, R.M.2    Neumann, D.A.3    Kisliuk, A.4    Sokolov, A.P.5    Liu, J.6    Yee, A.F.7    Wu, W.L.8
  • 73
    • 0035827151 scopus 로고    scopus 로고
    • Relaxation spectra in PMMA: Comparison of acoustic attenuation and light scattering data
    • Caliskan, G., A. Kisliuk, V. N. Novikov, and A. P. Sokolov. 2001. Relaxation spectra in PMMA: comparison of acoustic attenuation and light scattering data. J. Chem. Phys. 114:10189-10195.
    • (2001) J. Chem. Phys. , vol.114 , pp. 10189-10195
    • Caliskan, G.1    Kisliuk, A.2    Novikov, V.N.3    Sokolov, A.P.4
  • 74
    • 0000656973 scopus 로고
    • Neutron incoherent scattering law for diffusion in a potential of spherical symmetry: General formalism and application to diffusion inside a sphere
    • Volino, F., and A. J. Dianoux. 1980. Neutron incoherent scattering law for diffusion in a potential of spherical symmetry: general formalism and application to diffusion inside a sphere. Mol. Phys. 41:271-279.
    • (1980) Mol. Phys. , vol.41 , pp. 271-279
    • Volino, F.1    Dianoux, A.J.2
  • 75
    • 0003314497 scopus 로고
    • Thermodynamic and related studies of water interacting with proteins
    • Water in Polymers. S. P. Rowland, editor. American. Chemical. Society. Washington, DC
    • Rupley, J. A., P. H. Yang, and G. Tollin. 1980. Thermodynamic and related studies of water interacting with proteins. In Water in Polymers. ACS Symposium Series, Vol. 127. S. P. Rowland, editor. American. Chemical. Society. Washington, DC. 111-132.
    • (1980) ACS Symposium Series , vol.127 , pp. 111-132
    • Rupley, J.A.1    Yang, P.H.2    Tollin, G.3
  • 76
    • 4644278807 scopus 로고    scopus 로고
    • Enzyme catalysis of substrate vapor: Enzyme activity occurs at very low hydration
    • Lind, P. A., R. M. Daniel, C. Monk, and R. V. Dunn. 2004. Enzyme catalysis of substrate vapor: enzyme activity occurs at very low hydration. Biochim. Biophys. Acta. 1702:103-110.
    • (2004) Biochim. Biophys. Acta , vol.1702 , pp. 103-110
    • Lind, P.A.1    Daniel, R.M.2    Monk, C.3    Dunn, R.V.4
  • 77
    • 18644379953 scopus 로고    scopus 로고
    • Coupling between lysozyme and glycerol dynamics: Microscopic insights from molecular dynamics simulations
    • Dirama, T. E., G. A. Carri, and A. P. Sokolov. 2005. Coupling between lysozyme and glycerol dynamics: microscopic insights from molecular dynamics simulations. J. Chem. Phys. 122:244910.
    • (2005) J. Chem. Phys. , vol.122 , pp. 244910
    • Dirama, T.E.1    Carri, G.A.2    Sokolov, A.P.3
  • 78
    • 31144460588 scopus 로고    scopus 로고
    • Coupling between lysozyme and trehalose dynamics: Microscopic insights from molecular dynamics simulations
    • Dirama, T. E., J. E. Curtis, G. A. Carri, and A. P. Sokolov. 2006. Coupling between lysozyme and trehalose dynamics: microscopic insights from molecular dynamics simulations. J. Chem. Phys. 124:034901.
    • (2006) J. Chem. Phys. , vol.124 , pp. 034901
    • Dirama, T.E.1    Curtis, J.E.2    Carri, G.A.3    Sokolov, A.P.4


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