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Volumn 93, Issue 9, 2007, Pages 2986-3000

Influence of water clustering on the dynamics of hydration water at the surface of a lysozyme

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; WATER;

EID: 36048931839     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.108753     Document Type: Article
Times cited : (67)

References (103)
  • 1
    • 33750286994 scopus 로고    scopus 로고
    • Do we underestimate the importance of water in cell biology?
    • Chaplin, M. 2006. Do we underestimate the importance of water in cell biology? Nat. Rev. Mol. Cell Biol. 7:861-866.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 861-866
    • Chaplin, M.1
  • 2
    • 33745032291 scopus 로고    scopus 로고
    • Water mediation in protein folding and molecular recognition
    • Levy, Y., and J. N. Onuchic. 2006. Water mediation in protein folding and molecular recognition. Annu. Rev. Biophys. Biomol. Struct. 35:389-415.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 389-415
    • Levy, Y.1    Onuchic, J.N.2
  • 3
    • 33846417622 scopus 로고    scopus 로고
    • Protein dynamics tightly connected to the dynamics of surrounding and internal water molecules
    • Helms, V. 2007. Protein dynamics tightly connected to the dynamics of surrounding and internal water molecules. Chem. Phys. Chem. 8:23-33.
    • (2007) Chem. Phys. Chem , vol.8 , pp. 23-33
    • Helms, V.1
  • 4
    • 0016281436 scopus 로고
    • Interrelationships between water and metabolism in Artemia salina cysts: Hydration-dehydration from the liquid and vapor phases
    • Clegg, J. S. 1974. Interrelationships between water and metabolism in Artemia salina cysts: hydration-dehydration from the liquid and vapor phases. J. Exp. Biol. 61:291-308.
    • (1974) J. Exp. Biol , vol.61 , pp. 291-308
    • Clegg, J.S.1
  • 5
    • 0023641519 scopus 로고
    • Oxidative processes in soybean and pea seeds
    • Vertucci, C. W., and A. C. Leopold. 1987. Oxidative processes in soybean and pea seeds. Plant Physiol. 84:1038-1043.
    • (1987) Plant Physiol , vol.84 , pp. 1038-1043
    • Vertucci, C.W.1    Leopold, A.C.2
  • 6
    • 0018366224 scopus 로고
    • The effect of restricted hydration on the rate of reaction of glucose 6-phosphate dehydrogenase, phosphoglucose isomerase, hexokinase and fumarase
    • Stevens, E., and L. Stevens. 1979. The effect of restricted hydration on the rate of reaction of glucose 6-phosphate dehydrogenase, phosphoglucose isomerase, hexokinase and fumarase. Biochem. J. 179:161-167.
    • (1979) Biochem. J , vol.179 , pp. 161-167
    • Stevens, E.1    Stevens, L.2
  • 7
    • 0003314497 scopus 로고
    • Thermodynamic and related studies of water interacting with proteins
    • Water in Polymers, S. P. Rouland, 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. Rouland, editor. American Chemical Society, Washington, DC.
    • (1980) ACS Symposium Series , vol.127
    • Rupley, J.A.1    Yang, P.-H.2    Tollin, G.3
  • 9
    • 0022425369 scopus 로고
    • Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions
    • Schinkel, J. E., N. W. Downer, and J. A. Rupley. 1985. Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions. Biochemistry. 24:352-366.
    • (1985) Biochemistry , vol.24 , pp. 352-366
    • Schinkel, J.E.1    Downer, N.W.2    Rupley, J.A.3
  • 10
    • 13344250471 scopus 로고    scopus 로고
    • The role of hydration in enzyme activity and stability. 2. Alcohol dehydrogenase activity and stability in a continuous gas phase reactor
    • Yang, F., and A. J. Russel. 2000. The role of hydration in enzyme activity and stability. 2. Alcohol dehydrogenase activity and stability in a continuous gas phase reactor. Biotechnol. Bioeng. 49:709-716.
    • (2000) Biotechnol. Bioeng , vol.49 , pp. 709-716
    • Yang, F.1    Russel, A.J.2
  • 11
    • 4644278807 scopus 로고    scopus 로고
    • Esterase catalysis of substrate vapor: Enzyme activity occurs at very low hydration
    • Lind, P. A., R. M. Daniel, C. Monk, and R. V. Dunn. 2004. Esterase 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
  • 12
    • 4344717466 scopus 로고    scopus 로고
    • What can we learn by studying enzymes in non-aqueous media?
    • Halling, P. J. 2004. What can we learn by studying enzymes in non-aqueous media? Philos. Trans. R. Soc. Lond. B Biol. Sci. 359:1287-1297.
    • (2004) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.359 , pp. 1287-1297
    • Halling, P.J.1
  • 13
    • 0032555351 scopus 로고    scopus 로고
    • Function and picosecond dynamics of bacteriorhodopsin in purple membrane at different lipidation and hydration
    • Fitter, J., S. A. W. Verclas, R. E. Lechner, and N. A. Dencher. 1998. Function and picosecond dynamics of bacteriorhodopsin in purple membrane at different lipidation and hydration. FEBS Lett. 433:321-325.
    • (1998) FEBS Lett , vol.433 , pp. 321-325
    • Fitter, J.1    Verclas, S.A.W.2    Lechner, R.E.3    Dencher, N.A.4
  • 14
    • 0017764227 scopus 로고
    • Hydration effects on cis-trans isomerization of bacteriorhodopsin
    • Korenstein, R., and B. Hess. 1977. Hydration effects on cis-trans isomerization of bacteriorhodopsin. FEBS Lett. 82:7-11.
    • (1977) FEBS Lett , vol.82 , pp. 7-11
    • Korenstein, R.1    Hess, B.2
  • 15
    • 0020791844 scopus 로고
    • Photoelectric signals from dried oriented purple membranes of Halobacterium halobium
    • Varo, G., and L. Keszthelyi. 1983. Photoelectric signals from dried oriented purple membranes of Halobacterium halobium. Biophys. J. 43:47-51.
    • (1983) Biophys. J , vol.43 , pp. 47-51
    • Varo, G.1    Keszthelyi, L.2
  • 17
    • 0001763860 scopus 로고
    • Critical exponents of protonic percolation in hydrated lysozyme powders
    • Careri, G., A. Giansanti, and J. A. Rupley. 1988. Critical exponents of protonic percolation in hydrated lysozyme powders. Phys. Rev. A. 37:2703-2705.
    • (1988) Phys. Rev. A , vol.37 , pp. 2703-2705
    • Careri, G.1    Giansanti, A.2    Rupley, J.A.3
  • 18
    • 0035510439 scopus 로고    scopus 로고
    • Glassy dynamics and enzymatic activity of lysozyme
    • Pizzitutti, F., and F. Bruni. 2001. Glassy dynamics and enzymatic activity of lysozyme. Phys. Rev. E. 64:052905.
    • (2001) Phys. Rev. E , vol.64 , pp. 052905
    • Pizzitutti, F.1    Bruni, F.2
  • 19
    • 0000447482 scopus 로고
    • Critical exponents of protonic percolation in maize seeds
    • Bruni, F., G. Careri, and A. C. Leopold. 1989. Critical exponents of protonic percolation in maize seeds. Phys. Rev. A. 40:2803-2805.
    • (1989) Phys. Rev. A , vol.40 , pp. 2803-2805
    • Bruni, F.1    Careri, G.2    Leopold, A.C.3
  • 20
    • 0031143805 scopus 로고    scopus 로고
    • Dielectric investigation of the protonic conductivity in plant seeds
    • Konsta, A. A., J. Laudat, and P. Pissis. 1997. Dielectric investigation of the protonic conductivity in plant seeds. Solid State Ionics. 97:97-104.
    • (1997) Solid State Ionics , vol.97 , pp. 97-104
    • Konsta, A.A.1    Laudat, J.2    Pissis, P.3
  • 21
    • 41349122850 scopus 로고    scopus 로고
    • Water-network percolation transitions in hydrated yeast
    • Sokolowska, D., A. Krol-Otwinowska, and J. K. Moscicki. 2004. Water-network percolation transitions in hydrated yeast. Phys. Rev. E. 70:052901.
    • (2004) Phys. Rev. E , vol.70 , pp. 052901
    • Sokolowska, D.1    Krol-Otwinowska, A.2    Moscicki, J.K.3
  • 22
    • 36048974044 scopus 로고
    • Dielectric properties of Artemia cysts at low water contents. Evidence for a percolative transition
    • Bruni, F., G. Careri, and J. S. Clegg. 1990. Dielectric properties of Artemia cysts at low water contents. Evidence for a percolative transition. Biophys. J. 23:932-939.
    • (1990) Biophys. J , vol.23 , pp. 932-939
    • Bruni, F.1    Careri, G.2    Clegg, J.S.3
  • 23
    • 0345157270 scopus 로고
    • Two-dimensional protonic percolation on lightly hydrated purple membrane
    • Rupley, J. A., L. Siemankowski, G. Careri, and F. Bruni. 1988. Two-dimensional protonic percolation on lightly hydrated purple membrane. Proc. Natl. Acad. Sci. USA. 85:9022-9025.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9022-9025
    • Rupley, J.A.1    Siemankowski, L.2    Careri, G.3    Bruni, F.4
  • 26
    • 0026720247 scopus 로고
    • Crystalline ribonuclease A loses function below the dynamic transition at 220K
    • Rasmussen, B. F., A. M. Stock, D. Ringe, and G. A. Petsco. 1992. Crystalline ribonuclease A loses function below the dynamic transition at 220K. Nature. 357:423-424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsco, G.A.4
  • 28
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effect 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 membranes: effect 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
  • 29
    • 0033064923 scopus 로고    scopus 로고
    • The temperature dependence of internal molecular motion in hydrated and dry α-amylase: The role of hydration water in the dynamical transition of proteins
    • Fitter, J. 1999. The temperature dependence of internal molecular motion in hydrated and dry α-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
  • 30
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the environment on the protein dynamic transition: A neutron scattering study
    • Paciaroni, A., S. Cinemmi, and G. Onori. 2002. Effect of the environment on the protein dynamic transition: a neutron scattering study. Biophys. J. 83:1157-1164.
    • (2002) Biophys. J , vol.83 , pp. 1157-1164
    • Paciaroni, A.1    Cinemmi, S.2    Onori, G.3
  • 31
    • 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
  • 32
    • 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
  • 33
    • 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
  • 35
    • 11144307257 scopus 로고    scopus 로고
    • Fragile-to-strong liquid transition in deeply supercooled confined water
    • Faraone, A., L. Liu, C.-Y. Mou, C.-W. Yen, and S.-H. Chen. 2004. Fragile-to-strong liquid transition in deeply supercooled confined water. J. Chem. Phys. 121:10843-10846.
    • (2004) J. Chem. Phys , vol.121 , pp. 10843-10846
    • Faraone, A.1    Liu, L.2    Mou, C.-Y.3    Yen, C.-W.4    Chen, S.-H.5
  • 36
    • 27144463970 scopus 로고    scopus 로고
    • Pressure dependence of fragile-to-strong transition and a possible second critical point in supercooled confined water
    • Liu, L., S.-H. Chen, A. Faraone, C.-W. Yen, and C.-Y. Mou. 2005. Pressure dependence of fragile-to-strong transition and a possible second critical point in supercooled confined water. Phys. Rev. Lett. 95:117802.
    • (2005) Phys. Rev. Lett , vol.95 , pp. 117802
    • Liu, L.1    Chen, S.-H.2    Faraone, A.3    Yen, C.-W.4    Mou, C.-Y.5
  • 39
    • 28044455451 scopus 로고    scopus 로고
    • Relation between the Widom line and the dynamic crossover in systems with a liquid-liquid phase transition
    • Xu, L., P. Kumar, S. V. Buldyrev, S.-H. Chen, P. H. Poole, F. Sciortino, and H. E. Stanley. 2005. Relation between the Widom line and the dynamic crossover in systems with a liquid-liquid phase transition. Proc. Natl. Acad. Sci. USA. 102:16558-16562.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16558-16562
    • Xu, L.1    Kumar, P.2    Buldyrev, S.V.3    Chen, S.-H.4    Poole, P.H.5    Sciortino, F.6    Stanley, H.E.7
  • 40
    • 0018793861 scopus 로고
    • Temperature-dependent x-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder, H., G. A. Pestko, and D. Tsernoglou. 1979. Temperature-dependent x-ray diffraction as a probe of protein structural dynamics. Nature. 280:558-563.
    • (1979) Nature , vol.280 , pp. 558-563
    • Frauenfelder, H.1    Pestko, G.A.2    Tsernoglou, D.3
  • 41
    • 20444433942 scopus 로고
    • The study of energy-levels in biochemistry
    • Szent-Gyorgyi, A. 1941. The study of energy-levels in biochemistry. Nature. 3745:157-159.
    • (1941) Nature , vol.3745 , pp. 157-159
    • Szent-Gyorgyi, A.1
  • 43
    • 0005829624 scopus 로고
    • Dielectric properties of protein powders with adsorbed water
    • Rosen, D. 1963. Dielectric properties of protein powders with adsorbed water. Trans. Faraday Soc. 59:2178-2191.
    • (1963) Trans. Faraday Soc , vol.59 , pp. 2178-2191
    • Rosen, D.1
  • 44
    • 0015504345 scopus 로고
    • Dielectric relaxation spectra of water adsorbed at lysozyme
    • Harvey, S. C., and P. Hoekstra. 1972. Dielectric relaxation spectra of water adsorbed at lysozyme. J. Phys. Chem. 76:2987-2994.
    • (1972) J. Phys. Chem , vol.76 , pp. 2987-2994
    • Harvey, S.C.1    Hoekstra, P.2
  • 45
    • 0020490656 scopus 로고
    • Dielectric studies of the binding of water to lysozyme
    • Bone, S., and R. Pethig. 1982. Dielectric studies of the binding of water to lysozyme. J. Mol. Biol. 157:571-575.
    • (1982) J. Mol. Biol , vol.157 , pp. 571-575
    • Bone, S.1    Pethig, R.2
  • 46
    • 0022429109 scopus 로고
    • Dielectric studies of protein hydration and hydration-induced flexibility
    • Bone, S., and R. Pethig. 1985. Dielectric studies of protein hydration and hydration-induced flexibility. J. Mol. Biol. 181:323-326.
    • (1985) J. Mol. Biol , vol.181 , pp. 323-326
    • Bone, S.1    Pethig, R.2
  • 47
    • 0000324614 scopus 로고
    • Protonic conductivity of hydrated lysozyme powders at megahertz frequencies
    • Careri, G., M. Geraci, A. Giansanti, and J. A. Rupley. 1985. Protonic conductivity of hydrated lysozyme powders at megahertz frequencies. Proc. Natl. Acad. Sci. USA. 82:5342-5346.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5342-5346
    • Careri, G.1    Geraci, M.2    Giansanti, A.3    Rupley, J.A.4
  • 48
    • 0018356110 scopus 로고
    • Protein-water interactions. Heat capacity of the lysozyme-water system
    • Yang, P.-H., and J. A. Rupley. 1979. Protein-water interactions. Heat capacity of the lysozyme-water system. Biochemistry. 18:2654-2661.
    • (1979) Biochemistry , vol.18 , pp. 2654-2661
    • Yang, P.-H.1    Rupley, J.A.2
  • 49
    • 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
  • 50
    • 13444250015 scopus 로고    scopus 로고
    • Formation of spanning water networks on protein surfaces via 2D percolation transition
    • Oleinikova, A., N. Smolin, I. Brovchenko, A. Geiger, and R. Winter. 2005. Formation of spanning water networks on protein surfaces via 2D percolation transition. J. Phys. Chem. B. 109:1988-1998.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1988-1998
    • Oleinikova, A.1    Smolin, N.2    Brovchenko, I.3    Geiger, A.4    Winter, R.5
  • 51
    • 33244471517 scopus 로고    scopus 로고
    • Percolation transition of hydration water: From planar hydrophilic surfaces to proteins
    • Oleinikova, A., I. Brovchenko, N. Smolin, A. Krukau, A. Geiger, and R. Winter. 2005. Percolation transition of hydration water: from planar hydrophilic surfaces to proteins. Phys. Rev. Lett. 95:247802.
    • (2005) Phys. Rev. Lett , vol.95 , pp. 247802
    • Oleinikova, A.1    Brovchenko, I.2    Smolin, N.3    Krukau, A.4    Geiger, A.5    Winter, R.6
  • 53
    • 33750301285 scopus 로고    scopus 로고
    • Origin of the dynamic transition upon pressurization of crystalline proteins
    • Oleinikova, A., N. Smolin, and I. Brovchenko. 2006. Origin of the dynamic transition upon pressurization of crystalline proteins. J. Phys. Chem. B. 110:19619-19624.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 19619-19624
    • Oleinikova, A.1    Smolin, N.2    Brovchenko, I.3
  • 55
    • 33645159463 scopus 로고    scopus 로고
    • Percolation transition of hydration water at hydrophilic surfaces
    • Oleinikova, A., I. Brovchenko, and A. Geiger. 2006. Percolation transition of hydration water at hydrophilic surfaces. Physica A. 364:1-12.
    • (2006) Physica A , vol.364 , pp. 1-12
    • Oleinikova, A.1    Brovchenko, I.2    Geiger, A.3
  • 56
    • 34147149687 scopus 로고    scopus 로고
    • Percolation transition of hydration water in biosystems
    • Oleinikova, A., and I. Brovchenko. 2006. Percolation transition of hydration water in biosystems. Mol. Phys. 104:3841-3855.
    • (2006) Mol. Phys , vol.104 , pp. 3841-3855
    • Oleinikova, A.1    Brovchenko, I.2
  • 57
    • 33749337783 scopus 로고    scopus 로고
    • Water percolation governs polymorphic transitions and conductivity of DNA
    • Brovchenko, I., A. Krukau, A. Oleinikova, and A. K. Mazur. 2006. Water percolation governs polymorphic transitions and conductivity of DNA. Phys. Rev. Lett. 97:137801.
    • (2006) Phys. Rev. Lett , vol.97 , pp. 137801
    • Brovchenko, I.1    Krukau, A.2    Oleinikova, A.3    Mazur, A.K.4
  • 58
    • 34249993788 scopus 로고    scopus 로고
    • Molecular organization of gases and liquids at solid surfaces
    • Chapt. 3. American Scientific Publishers, Stevenson Ranch, CA
    • Brovchenko, I., and A. Oleinikova. 2006. Molecular organization of gases and liquids at solid surfaces. In Handbook of Theoretical and Computational Nanotechnology, Vol. 9, Chapt. 3. American Scientific Publishers, Stevenson Ranch, CA.
    • (2006) Handbook of Theoretical and Computational Nanotechnology , vol.9
    • Brovchenko, I.1    Oleinikova, A.2
  • 60
    • 0344863187 scopus 로고    scopus 로고
    • Thermal motion of bacteriorhodopsin at different hydration levels
    • Lehnert, U., V. Reat, M. Weik, G. Zaccai, and C. Pfister. 1998. Thermal motion of bacteriorhodopsin at different hydration levels. Biophys. J. 75:1945-1952.
    • (1998) Biophys. J , vol.75 , pp. 1945-1952
    • Lehnert, U.1    Reat, V.2    Weik, M.3    Zaccai, G.4    Pfister, C.5
  • 61
    • 2742571585 scopus 로고    scopus 로고
    • Slow dynamics of water molecules on the surface of a globular protein
    • Bellissent-Funel, M.-C., J.-M. Zanotti, and S. H. Chen. 1996. Slow dynamics of water molecules on the surface of a globular protein. Faraday Discuss. 103:281-294.
    • (1996) Faraday Discuss , vol.103 , pp. 281-294
    • Bellissent-Funel, M.-C.1    Zanotti, J.-M.2    Chen, S.H.3
  • 62
    • 0034662841 scopus 로고    scopus 로고
    • Relaxational dynamics of water molecules at protein surface
    • Dellerue, S., and M.-C. Bellissent-Funel. 2000. Relaxational dynamics of water molecules at protein surface. Chem. Phys. 258:315-325.
    • (2000) Chem. Phys , vol.258 , pp. 315-325
    • Dellerue, S.1    Bellissent-Funel, M.-C.2
  • 64
    • 0036708465 scopus 로고    scopus 로고
    • A model for water motion in crystals of lysozyme based on an incoherent quasielastic neutron-scattering study
    • Bon, C., A. J. Dianoux, M. Ferrand, and M. S. Lehmann. 2002. A model for water motion in crystals of lysozyme based on an incoherent quasielastic neutron-scattering study. Biophys. J. 83:1578-1588.
    • (2002) Biophys. J , vol.83 , pp. 1578-1588
    • Bon, C.1    Dianoux, A.J.2    Ferrand, M.3    Lehmann, M.S.4
  • 65
    • 0000013977 scopus 로고    scopus 로고
    • Molecular dynamics simulation evidence of anomalous diffusion of protein hydration water
    • Bizzarri, A., and S. Cannistraro. 1996. Molecular dynamics simulation evidence of anomalous diffusion of protein hydration water. Phys. Rev. E. 53:R3040-R3043.
    • (1996) Phys. Rev. E , vol.53
    • Bizzarri, A.1    Cannistraro, S.2
  • 66
    • 0030582803 scopus 로고    scopus 로고
    • Origin of the anomalous diffusion observed by MD simulation at the protein-water interface
    • Bizzarri, A., C. Rocchi, and S. Cannistraro. 1996. Origin of the anomalous diffusion observed by MD simulation at the protein-water interface. Chem. Phys. Lett. 263:559-566.
    • (1996) Chem. Phys. Lett , vol.263 , pp. 559-566
    • Bizzarri, A.1    Rocchi, C.2    Cannistraro, S.3
  • 67
    • 0033637521 scopus 로고    scopus 로고
    • The dynamics of protein hydration water: A quantitative comparison of molecular dynamic simulations and neutron-scattering experiments
    • Tarek, M., and D. Tobias. 2000. The dynamics of protein hydration water: a quantitative comparison of molecular dynamic simulations and neutron-scattering experiments. Biophys. J. 79:3244-3275.
    • (2000) Biophys. J , vol.79 , pp. 3244-3275
    • Tarek, M.1    Tobias, D.2
  • 68
    • 0037067102 scopus 로고    scopus 로고
    • Water rotational relaxation and diffusion in hydrated lysozyme
    • Marchi, M., F. Sterpone, and M. Ceccarelli. 2002. Water rotational relaxation and diffusion in hydrated lysozyme. J. Am. Chem. Soc. 124:6787-6791.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6787-6791
    • Marchi, M.1    Sterpone, F.2    Ceccarelli, M.3
  • 69
    • 0018473089 scopus 로고
    • Lysozyme film hydration events: An IR and gravimetric study
    • Careri, G., A. Giansanti, and E. Gratton. 1979. Lysozyme film hydration events: an IR and gravimetric study. Biopolymers. 18:1187-1203.
    • (1979) Biopolymers , vol.18 , pp. 1187-1203
    • Careri, G.1    Giansanti, A.2    Gratton, E.3
  • 70
    • 0025465003 scopus 로고
    • Protonic percolation on hydrated lysozyme powders studied by the method of thermally stimulated depolarization currents
    • Pissis, P., and A. Anagnostopoulou-Konsta. 1990. Protonic percolation on hydrated lysozyme powders studied by the method of thermally stimulated depolarization currents. J. Phys. D: Appl. Phys. 23:932-939.
    • (1990) J. Phys. D: Appl. Phys , vol.23 , pp. 932-939
    • Pissis, P.1    Anagnostopoulou-Konsta, A.2
  • 71
    • 0031933914 scopus 로고    scopus 로고
    • Low-frequency Raman spectra of lysozyme crystals and oriented DNA films: Dynamics of crystal water
    • Urabe, H., Y. Sugawara, M. Ataka, and A. Ruppecht. 1998. Low-frequency Raman spectra of lysozyme crystals and oriented DNA films: dynamics of crystal water. Biophys. J. 74:1533-1540.
    • (1998) Biophys. J , vol.74 , pp. 1533-1540
    • Urabe, H.1    Sugawara, Y.2    Ataka, M.3    Ruppecht, A.4
  • 72
    • 0037459120 scopus 로고    scopus 로고
    • A percolation transition cluster model of the temperature dependent dielectric properties of hydrated proteins
    • Suherman, P. M., and G. Smith. 2003. A percolation transition cluster model of the temperature dependent dielectric properties of hydrated proteins. J. Phys. D: Appl. Phys. 36:336-342.
    • (2003) J. Phys. D: Appl. Phys , vol.36 , pp. 336-342
    • Suherman, P.M.1    Smith, G.2
  • 73
    • 4043050078 scopus 로고    scopus 로고
    • Thermal stability and internal dynamics of lysozyme as affected by hydration
    • Cinelli, S., A. D. Francesco, G. Onori, and A. Paciaroni. 2004. Thermal stability and internal dynamics of lysozyme as affected by hydration. Phys. Chem. Chem. Phys. 6:3591-3595.
    • (2004) Phys. Chem. Chem. Phys , vol.6 , pp. 3591-3595
    • Cinelli, S.1    Francesco, A.D.2    Onori, G.3    Paciaroni, A.4
  • 74
    • 33646170638 scopus 로고    scopus 로고
    • Hydration dependence of conformational dielectric relaxation of lysozyme
    • Knab, J., J.-Y. Chen, and A. Markelz. 2006. Hydration dependence of conformational dielectric relaxation of lysozyme. Biophys. J. 90:2576-2581.
    • (2006) Biophys. J , vol.90 , pp. 2576-2581
    • Knab, J.1    Chen, J.-Y.2    Markelz, A.3
  • 76
    • 13444304312 scopus 로고    scopus 로고
    • Hydration-dependent internal dynamics of macromolecules: A neutron scattering study
    • Cinelli, S., M. Freda, G. Onori, A. Paciaroni, and A. Santucci. 2005. Hydration-dependent internal dynamics of macromolecules: a neutron scattering study. J. Mol. Liquids. 117:99-105.
    • (2005) J. Mol. Liquids , vol.117 , pp. 99-105
    • Cinelli, S.1    Freda, M.2    Onori, G.3    Paciaroni, A.4    Santucci, A.5
  • 77
    • 0025811817 scopus 로고
    • Lysozyme and A-lactalbumin: Structure, function and interrelationships
    • McKenzie, H. A., and F. H. J. White. 1991. Lysozyme and A-lactalbumin: structure, function and interrelationships. Adv. Protein Chem. 41:174-315.
    • (1991) Adv. Protein Chem , vol.41 , pp. 174-315
    • McKenzie, H.A.1    White, F.H.J.2
  • 79
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • Kundrot, C. E., and F. M. Richards. 1987. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J. Mol. Biol. 193:157-170.
    • (1987) J. Mol. Biol , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 84
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nose, S. 1984. A molecular dynamics method for simulations in the canonical ensemble. Mol. Phys. 52:255-268.
    • (1984) Mol. Phys , vol.52 , pp. 255-268
    • Nose, S.1
  • 85
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. 1985. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. A. 31:1695-1697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 87
    • 0345498055 scopus 로고    scopus 로고
    • Anomalous diffusion of the adsorbed water: A neutron scattering study of hydrated myoglobin
    • Settles, M., and W. Doster. 1996. Anomalous diffusion of the adsorbed water: a neutron scattering study of hydrated myoglobin. Faraday Discuss. 103:269-279.
    • (1996) Faraday Discuss , vol.103 , pp. 269-279
    • Settles, M.1    Doster, W.2
  • 88
    • 0001030002 scopus 로고    scopus 로고
    • Water dynamical anomalies evidences by molecular dynamics simulations at the solvent-protein
    • Rocchi, C., A. R. Bizzarri, and S. Cannistraro. 1998. Water dynamical anomalies evidences by molecular dynamics simulations at the solvent-protein. Phys. Rev. E. 57:3315-3325.
    • (1998) Phys. Rev. E , vol.57 , pp. 3315-3325
    • Rocchi, C.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 89
    • 0031807764 scopus 로고    scopus 로고
    • Diffusion of solvent around biomolecular solutes: A molecular dynamics simulation study
    • Makarov, V. A., M. Feig, B. K. Andrews, and B. M. Pettitt. 1998. Diffusion of solvent around biomolecular solutes: a molecular dynamics simulation study. Biophys. J. 75:150-158.
    • (1998) Biophys. J , vol.75 , pp. 150-158
    • Makarov, V.A.1    Feig, M.2    Andrews, B.K.3    Pettitt, B.M.4
  • 90
    • 0343614206 scopus 로고    scopus 로고
    • A systematic study of water models for molecular simulation: Derivation of water models optimized for use with a reaction field
    • van der Spoel, D., P. J. van Maaren, and H. J. C. Berendsen. 1998. A systematic study of water models for molecular simulation: derivation of water models optimized for use with a reaction field. J. Chem. Phys. 108:10220-10230.
    • (1998) J. Chem. Phys , vol.108 , pp. 10220-10230
    • van der Spoel, D.1    van Maaren, P.J.2    Berendsen, H.J.C.3
  • 91
    • 84908462885 scopus 로고
    • Theory of the electrical residue in the Leiden bottle
    • Kohlrausch, R. 1854. Theory of the electrical residue in the Leiden bottle. Pogg. Ann. Phys. Chem. 91:179-214.
    • (1854) Pogg. Ann. Phys. Chem , vol.91 , pp. 179-214
    • Kohlrausch, R.1
  • 92
    • 0014699523 scopus 로고
    • Non-symmetrical dielectric relaxation behavior arising from a simple empirical decay function
    • Williams, G., and D. C. Watts. 1970. Non-symmetrical dielectric relaxation behavior arising from a simple empirical decay function. Trans. Faraday Soc. 66:80-85.
    • (1970) Trans. Faraday Soc , vol.66 , pp. 80-85
    • Williams, G.1    Watts, D.C.2
  • 93
    • 33244458851 scopus 로고    scopus 로고
    • Pressure-dependent transition in protein dynamics at about 4 kbar revealed by molecular dynamics simulation
    • Meinhold, L., and J. C. Smith. 2005. Pressure-dependent transition in protein dynamics at about 4 kbar revealed by molecular dynamics simulation. Phys. Rev. E. 72:061908.
    • (2005) Phys. Rev. E , vol.72 , pp. 061908
    • Meinhold, L.1    Smith, J.C.2
  • 94
    • 36549100616 scopus 로고
    • Fluids in micro-pores. II. Self-diffusion in a simple classical fluid in a slit pore
    • Schoen, M., J. H. Cushman, D. J. Diestler, and C. L. Rhykerd, Jr. 1988. Fluids in micro-pores. II. Self-diffusion in a simple classical fluid in a slit pore. J. Chem. Phys. 88:1394-1406.
    • (1988) J. Chem. Phys , vol.88 , pp. 1394-1406
    • Schoen, M.1    Cushman, J.H.2    Diestler, D.J.3    Rhykerd Jr., C.L.4
  • 95
    • 0345393231 scopus 로고    scopus 로고
    • Phase coexistence and dynamic properties of water in nanopores
    • Brovchenko, I., A. Geiger, A. Oleinikova, and D. Paschek. 2003. Phase coexistence and dynamic properties of water in nanopores. Eur. Phys. J. E. 12:69-76.
    • (2003) Eur. Phys. J. E , vol.12 , pp. 69-76
    • Brovchenko, I.1    Geiger, A.2    Oleinikova, A.3    Paschek, D.4
  • 96
    • 28844443262 scopus 로고    scopus 로고
    • Diffusion of water in confined geometry: The case of a multilamellar bilayer
    • Sega, M., R. Vallauri, and S. Melchionna. 2005. Diffusion of water in confined geometry: the case of a multilamellar bilayer. Phys. Rev. E. 72:041201.
    • (2005) Phys. Rev. E , vol.72 , pp. 041201
    • Sega, M.1    Vallauri, R.2    Melchionna, S.3
  • 97
    • 0345328107 scopus 로고    scopus 로고
    • Anomalous dynamics of confined water at low hydration
    • Gallo, P., and M. Rovere. 2003. Anomalous dynamics of confined water at low hydration. J. Phys.: Condens. Matter. 15:7625-7633.
    • (2003) J. Phys.: Condens. Matter , vol.15 , pp. 7625-7633
    • Gallo, P.1    Rovere, M.2
  • 98
    • 21144445386 scopus 로고    scopus 로고
    • Diffusion of water and sodium counterions in nanopores of a β-lactoglobulin crystal: A molecular dynamics study
    • Malek, K., T. Odijk, and M.-O. Coppens. 2005. Diffusion of water and sodium counterions in nanopores of a β-lactoglobulin crystal: a molecular dynamics study. Nanotechnology. 16:S522-S530.
    • (2005) Nanotechnology , vol.16
    • Malek, K.1    Odijk, T.2    Coppens, M.-O.3
  • 99
    • 18144370104 scopus 로고    scopus 로고
    • Fluidity of hydration layers nanoconfined between mica surfaces
    • Leng, Y., and P. T. Cummings. 2005. Fluidity of hydration layers nanoconfined between mica surfaces. Phys. Rev. Lett. 94:026101.
    • (2005) Phys. Rev. Lett , vol.94 , pp. 026101
    • Leng, Y.1    Cummings, P.T.2
  • 100
    • 32444440762 scopus 로고    scopus 로고
    • A molecular jump mechanism of water reorientation
    • Laage, D., and J. T. Hynes. 2006. A molecular jump mechanism of water reorientation. Science. 311:832-835.
    • (2006) Science , vol.311 , pp. 832-835
    • Laage, D.1    Hynes, J.T.2
  • 101
    • 0027016652 scopus 로고
    • Protein-water interactions determined by dielectric methods
    • Pethig, R. 1992. Protein-water interactions determined by dielectric methods. Annu. Rev. Phys. Chem. 43:177-205.
    • (1992) Annu. Rev. Phys. Chem , vol.43 , pp. 177-205
    • Pethig, R.1
  • 102
    • 0029901852 scopus 로고    scopus 로고
    • Dielectric and gravimetric studied of water binding to lysozyme
    • Bone, S. 1996. Dielectric and gravimetric studied of water binding to lysozyme. Phys. Med. Biol. 41:1265-1275.
    • (1996) Phys. Med. Biol , vol.41 , pp. 1265-1275
    • Bone, S.1
  • 103
    • 0342394897 scopus 로고
    • The dielectric polarization of polar liquids
    • Kirkwood, J. G. 1939. The dielectric polarization of polar liquids. J. Chem. Phys. 7:911-919.
    • (1939) J. Chem. Phys , vol.7 , pp. 911-919
    • Kirkwood, J.G.1


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