메뉴 건너뛰기




Volumn 6, Issue SUPPL. 5, 2009, Pages

Coupled relaxations at the protein-water interface in the picosecond time scale

Author keywords

Anomalous diffusion; Hydration water; Maltose binding protein; Neutron scattering

Indexed keywords

HYDROGEN; MALTOSE; NEUTRON DIFFRACTION; NEUTRON SCATTERING; NEUTRONS;

EID: 69949151736     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2009.0182.focus     Document Type: Conference Paper
Times cited : (28)

References (37)
  • 1
    • 0009071257 scopus 로고
    • Formation of glasses from liquids and biopolymers
    • doi:10.1126/science.267.5206.1924
    • Angell, C. A. 1995 Formation of glasses from liquids and biopolymers. Science 267, 1924-1935. (doi:10.1126/science.267.5206.1924)
    • (1995) Science , vol.267 , pp. 1924-1935
    • Angell, C.A.1
  • 2
    • 38849196324 scopus 로고    scopus 로고
    • Water as an active constituent in cell biology
    • doi:10.1021/cr068037a
    • Ball, P. 2008 Water as an active constituent in cell biology. Chem. Rev. 108, 74-108. (doi:10.1021/cr068037a)
    • (2008) Chem. Rev. , vol.108 , pp. 74-108
    • Ball, P.1
  • 4
    • 0034257988 scopus 로고    scopus 로고
    • Glasslike dynamical behavior of the plastocyanin hydration water
    • doi:10.1103/PhysRevE.62.3991
    • Bizzarri, A. R., Paciaroni, A. & Cannistraro, S. 2000 Glasslike dynamical behavior of the plastocyanin hydration water. Phys. Rev. E 62, 3991-3999. (doi:10.1103/PhysRevE.62.3991)
    • (2000) Phys. Rev. E , vol.62 , pp. 3991-3999
    • Bizzarri, A.R.1    Paciaroni, A.2    Cannistraro, S.3
  • 5
    • 33745193035 scopus 로고    scopus 로고
    • Observation of fragile-to-strong dynamic crossover in protein hydration water
    • doi:10.1073/pnas.0602474103
    • Chen, S.-H., Liu, L., Fratini, E., Baflioni, P., Faraone, A. & Mamontov, E. 2006 Observation of fragile-to-strong dynamic crossover in protein hydration water. Proc. Natl Acad. Sci. USA 103, 9012-9016. (doi:10.1073/pnas. 0602474103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9012-9016
    • Chen, S.-H.1    Liu, L.2    Fratini, E.3    Baflioni, P.4    Faraone, A.5    Mamontov, E.6
  • 6
    • 28844473534 scopus 로고    scopus 로고
    • Picosecond-time- scale fluctuations of proteins in glassy matrices: The role of viscosity
    • doi:10.1103/PhysRevLett.95.158104
    • Cornicchi, E., Onori, G. & Paciaroni, A. 2005 Picosecond-time- scale fluctuations of proteins in glassy matrices: the role of viscosity. Phys. Rev. Lett. 95, 158 104-158 108. (doi:10.1103/PhysRevLett.95.158104)
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 158104-158108
    • Cornicchi, E.1    Onori, G.2    Paciaroni, A.3
  • 7
    • 0025333959 scopus 로고
    • Temperature dependence of the low frequency dynamics of myoglobin. Measurement of the vibrational frequency distribution by inelastic neutron scattering
    • doi:10.1016/S0006-3495(90)82369-9
    • 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. (doi:10.1016/S0006-3495(90)82369-9)
    • (1990) Biophys. J. , vol.58 , pp. 243-251
    • Cusack, S.1    Doster, W.2
  • 8
    • 0030862281 scopus 로고    scopus 로고
    • Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering
    • Diehl, M., Doster, W., Petry, W. & Shober, H. 1997 Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering. Biophys. J. 73, 2726-2732. (doi:10.1016/S0006-3495(97)78301-2) (Pubitemid 27471481)
    • (1997) Biophysical Journal , vol.73 , Issue.5 , pp. 2726-2732
    • Diehl, M.1    Doster, W.2    Petry, W.3    Schober, H.4
  • 9
    • 0001706226 scopus 로고
    • Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering
    • doi:10.1103/PhysRevLett.65.1080
    • 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, 1080-1083. (doi:10.1103/PhysRevLett.65.1080)
    • (1990) Phys. Rev. Lett. , vol.65 , pp. 1080-1083
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 10
    • 84956276384 scopus 로고
    • A unified model for the low-energy vibrational behaviour of amorphous solids
    • doi:10.1209/0295-5075/19/3/009
    • Elliott, S. R. 1992 A unified model for the low-energy vibrational behaviour of amorphous solids. Europhys. Lett. 19, 201-206. (doi:10.1209/0295- 5075/19/3/009)
    • (1992) Europhys. Lett. , vol.19 , pp. 201-206
    • Elliott, S.R.1
  • 11
    • 0000610350 scopus 로고
    • Change of the vibrational dynamics near the glass transition in polyisobutylene: Inelastic neutron scattering on a nonfragile polymer
    • doi:10.1103/PhysRevB.47.14795
    • Frick, B. & Richter, D. 1993 Change of the vibrational dynamics near the glass transition in polyisobutylene: inelastic neutron scattering on a nonfragile polymer. Phys. Rev. B 47, 14 795-14 804. (doi:10.1103/PhysRevB.47. 14795)
    • (1993) Phys. Rev. B , vol.47 , pp. 14795-14804
    • Frick, B.1    Richter, D.2
  • 12
    • 0000594431 scopus 로고
    • Primary relaxation in a hard sphere system
    • doi:10.1103/PhysRevA.45.898
    • Fuchs, M., Hofacker, I. & Latz, A. 1992 Primary relaxation in a hard sphere system. Phys. Rev. A 45, 898-902. (doi:10.1103/PhysRevA.45.898)
    • (1992) Phys. Rev. A , vol.45 , pp. 898-902
    • Fuchs, M.1    Hofacker, I.2    Latz, A.3
  • 13
    • 0011507803 scopus 로고    scopus 로고
    • The essentials of the mode-coupling theory for glassy dynamics
    • Gotze, W. 1998 The essentials of the mode-coupling theory for glassy dynamics. Condens. Matter Phys. 4, 873-904.
    • (1998) Condens. Matter Phys. , vol.4 , pp. 873-904
    • Gotze, W.1
  • 15
    • 0001755254 scopus 로고
    • Glassy behavior of a protein
    • doi:10.1103/PhysRevLett.62.1916
    • Iben, I. E. T. et al. 1989 Glassy behavior of a protein. Phys. Rev. Lett. 62, 1916-1919. (doi:10.1103/PhysRevLett.62.1916)
    • (1989) Phys. Rev. Lett. , vol.62 , pp. 1916-1919
    • Iben, I.E.T.1
  • 17
    • 55549086517 scopus 로고    scopus 로고
    • Dynamics at the protein water interface from 17O spin relaxation in deeply supercooled solutions
    • doi:10.1529/biophysj.108.135194
    • Mattea, C., Qvist, J. & Halle, B. 2008 Dynamics at the protein water interface from 17O spin relaxation in deeply supercooled solutions. Biophys. J 95, 2951-2963. (doi:10.1529/biophysj.108.135194)
    • (2008) Biophys. J , vol.95 , pp. 2951-2963
    • Mattea, C.1    Qvist, J.2    Halle, B.3
  • 18
    • 31944438519 scopus 로고    scopus 로고
    • Maltose-binding protein: A versatile platform for prototyping biosensing
    • doi:10.1016/j.copbio.2006.01.002
    • Medintz, I. L. & Deschamps, J. R. 2006 Maltose-binding protein: a versatile platform for prototyping biosensing. Curr. Opin. Biotech. 17, 17-27. (doi:10.1016/j.copbio.2006.01.002)
    • (2006) Curr. Opin. Biotech. , vol.17 , pp. 17-27
    • Medintz, I.L.1    Deschamps, J.R.2
  • 19
    • 43249110336 scopus 로고    scopus 로고
    • Subdiffusion in peptides originates from the fractal-like structure of configuration space
    • Nesius, T., Didone, I., Sokolov, I. M. & Smith, J. C. 2008 Subdiffusion in peptides originates from the fractal-like structure of configuration space. Phys. Rev. Lett. 100, 188 103.
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 188103
    • Nesius, T.1    Didone, I.2    Sokolov, I.M.3    Smith, J.C.4
  • 20
    • 67949118698 scopus 로고    scopus 로고
    • Collective dynamics of protein hydration water by brillouin neutron spectroscopy
    • doi:10.1021/ja807957p
    • Orecchini, A., Paciaroni, A., De Francesco, A., Petrillo, C. & Sacchetti, F. 2009 Collective dynamics of protein hydration water by brillouin neutron spectroscopy. J. Am. Chem. Soc 131, 4664-4669. (doi:10.1021/ja807957p)
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 4664-4669
    • Orecchini, A.1    Paciaroni, A.2    De Francesco, A.3    Petrillo, C.4    Sacchetti, F.5
  • 21
    • 0032873476 scopus 로고    scopus 로고
    • Incoherent neutron scattering of copper azurin: A comparison with molecular dynamics simulation results
    • Paciaroni, A., Stroppolo, M. E., Arcangeli, C., Bizzarri, A. R., Desideri, A. & Cannistraro, S. 1999 Incoherent neutron scattering of copper azurin: a comparison with molecular dynamics simulation results. Biophys. J. 28, 447-456.
    • (1999) Biophys. J. , vol.28 , pp. 447-456
    • Paciaroni, A.1    Stroppolo, M.E.2    Arcangeli, C.3    Bizzarri, A.R.4    Desideri, A.5    Cannistraro, S.6
  • 22
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the environment on the protein dynamical transition: A neutron scattering study
    • Paciaroni, A., Cinelli, S. & Onori, G. 2002 Effect of the environment on the protein dynamical transition: a neutron scattering study. Biophys. J. 83, 1157-1164. (doi:10.1016/S0006-3495(02)75239-9) (Pubitemid 34803646)
    • (2002) Biophysical Journal , vol.83 , Issue.2 , pp. 1157-1164
    • Paciaroni, A.1    Cinelli, S.2    Onori, G.3
  • 23
    • 53549094650 scopus 로고    scopus 로고
    • Fingerprints of amorphous icelike behavior in the vibrational density of states of protein hydration water
    • doi:10.1103/PhysRevLett.101.148104
    • Paciaroni, A. et al. 2008 Fingerprints of amorphous icelike behavior in the vibrational density of states of protein hydration water. Phys. Rev. Lett. 101, 148 104-148 108. (doi:10.1103/PhysRevLett.101.148104)
    • (2008) Phys. Rev. Lett. , vol.101 , pp. 148104-148108
    • Paciaroni, A.1
  • 24
    • 69949162150 scopus 로고
    • ed. M. A. Nusimovic, Paris, France: Flammarion
    • Renker, B. 1971 International conference on phonons (ed. M. A. Nusimovic), pp. 167-170. Paris, France: Flammarion.
    • (1971) International Conference on Phonons , pp. 167-170
    • Renker, B.1
  • 26
    • 4244155547 scopus 로고    scopus 로고
    • Amorphous polymorphism in ice investigated by inelastic neutron scattering
    • doi:10.1016/S0921-4526(97)00749-7
    • Schober, H., Koza, M., Tölle, A., Fujara, F., Angell, C. A. & Böhmer, R. 1998 Amorphous polymorphism in ice investigated by inelastic neutron scattering. Phys. B Cond. Matt. 897, 241-243. (doi:10.1016/S0921- 4526(97)00749-7)
    • (1998) Phys. B Cond. Matt. , vol.897 , pp. 241-243
    • Schober, H.1    Koza, M.2    Tölle, A.3    Fujara, F.4    Angell, C.A.5    Böhmer, R.6
  • 27
    • 0000289451 scopus 로고    scopus 로고
    • Supercooled water and the kinetic glass transition
    • doi:10.1103/PhysRevE.54.6331
    • Sciortino, F., Gallo, P., Tartaglia, P. & Chen, S.-H. 1996 Supercooled water and the kinetic glass transition. Phys. Rev. E 54, 6331-6343. (doi:10.1103/PhysRevE.54.6331)
    • (1996) Phys. Rev. E , vol.54 , pp. 6331-6343
    • Sciortino, F.1    Gallo, P.2    Tartaglia, P.3    Chen, S.-H.4
  • 28
    • 0345498055 scopus 로고    scopus 로고
    • Anomalous diffusion of adsorbed water: A neutron scattering study of hydrated myoglobin
    • Settles, M. & Doster, W. 1996 Anomalous diffusion of adsorbed water: a neutron scattering study of hydrated myoglobin. Faraday Discuss. 103, 269-279. (doi:10.1039/fd9960300269) (Pubitemid 126459160)
    • (1996) Faraday Discussions , vol.103 , pp. 269-279
    • Settles, M.1    Doster, W.2
  • 29
    • 0001726841 scopus 로고
    • Dynamics of super-cooled water: Mode-coupling theory approach
    • doi:10.1103/PhysRevB.51.12865
    • Sokolov, A., Hurst, J. & Quitmann, A. 1995 Dynamics of super-cooled water: mode-coupling theory approach. Phys. Rev. B 51, 12 865-12 868. (doi:10.1103/PhysRevB.51.12865)
    • (1995) Phys. Rev. B , vol.51 , pp. 12865-12868
    • Sokolov, A.1    Hurst, J.2    Quitmann, A.3
  • 30
    • 0000409076 scopus 로고    scopus 로고
    • Glassy dynamics in DNA: Ruled by water of hydration?
    • doi:10.1063/1.478610
    • Sokolov, A., Grimm, H. & Kahn, R. 1999 Glassy dynamics in DNA: ruled by water of hydration? J. Chem. Phys 110, 7053-7057. (doi:10.1063/1.478610)
    • (1999) J. Chem. Phys , vol.110 , pp. 7053-7057
    • Sokolov, A.1    Grimm, H.2    Kahn, R.3
  • 31
    • 0025754301 scopus 로고
    • The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G. Y. & Quiocho, F. A. 1991 The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-15019
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-15019
    • Spurlino, J.C.1    Lu, G.Y.2    Quiocho, F.A.3
  • 32
    • 0035879037 scopus 로고    scopus 로고
    • Effects of solvent damping on side chain and backbone contributions to the protein boson peak
    • doi:10.1063/1.1380708
    • Tarek, M. & Tobias, D. J. 2001 Effects of solvent damping on side chain and backbone contributions to the protein boson peak. J. Chem. Phys. 115, 1607-1612. (doi:10.1063/1.1380708)
    • (2001) J. Chem. Phys. , vol.115 , pp. 1607-1612
    • Tarek, M.1    Tobias, D.J.2
  • 33
    • 19044399611 scopus 로고    scopus 로고
    • Role of protein-water hydrogen bond dynamics in the protein dynamical transition
    • doi:10.1103/PhysRevLett.88.138101
    • Tarek, M. & Tobias, D. J. 2002 Role of protein-water hydrogen bond dynamics in the protein dynamical transition. Phys. Rev. Lett. 88, 138 101-138 105. (doi:10.1103/PhysRevLett.88.138101)
    • (2002) Phys. Rev. Lett. , vol.88 , pp. 138101-138105
    • Tarek, M.1    Tobias, D.J.2
  • 34
    • 0033988125 scopus 로고    scopus 로고
    • Solvent mobility and the protein 'glass' transition
    • doi:10.1038/71231
    • Vitkup, D., Ringe, D., Petsko, G. A. & Karplus, M. 2000 Solvent mobility and the protein 'glass' transition. Nat. Struct. Biol. 7, 34-38. (doi:10.1038/71231)
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 34-38
    • Vitkup, D.1    Ringe, D.2    Petsko, G.A.3    Karplus, M.4
  • 35
    • 33748526213 scopus 로고    scopus 로고
    • Low-frequency Raman Scattering from Water at High Pressures and High Temperature
    • doi:10.1021/jp960140o
    • Walrafen, G. E., Chu, Y. C. & Piermarini, G. J. 1996 Low-frequency Raman Scattering from Water at High Pressures and High Temperature. J. Phys. Chem. 100, 10 363-10 372. (doi:10.1021/jp960140o)
    • (1996) J. Phys. Chem. , vol.100 , pp. 10363-10372
    • Walrafen, G.E.1    Chu, Y.C.2    Piermarini, G.J.3
  • 36
    • 27744477788 scopus 로고    scopus 로고
    • Liquid-like water confined in stacks of biological membranes at 200 K and its relation to protein dynamics
    • DOI 10.1529/biophysj.104.055749
    • Weik, M., Lehnert, U. & Zaccai, G. 2005 Liquid-like water confined in stacks of biological membranes at 200 K and its relation to protein dynamics. Biophys. J. 89, 3639-3646. (doi:10.1529/biophysj.104.055749) (Pubitemid 41637971)
    • (2005) Biophysical Journal , vol.89 , Issue.5 , pp. 3639-3646
    • Weik, M.1    Lehnert, U.2    Zaccai, G.3
  • 37
    • 41849097415 scopus 로고    scopus 로고
    • Coincidence of dynamical transitions in a soluble protein and its hydration water: Direct measurements by neutron scattering and MD simulations
    • doi:10.1021/ja710526r
    • Wood, K., Frolich, A., Paciaroni, A., Moulin, M., Härtlein, M., Zaccaï, G., Tobias, D. J. & Weik, M. 2008 Coincidence of dynamical transitions in a soluble protein and its hydration water: direct measurements by neutron scattering and MD simulations. J. Am. Chem. Soc. 130, 4586-4587. (doi:10.1021/ja710526r)
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 4586-4587
    • Wood, K.1    Frolich, A.2    Paciaroni, A.3    Moulin, M.4    Härtlein, M.5    Zaccaï, G.6    Tobias, D.J.7    Weik, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.