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Volumn 95, Issue 2, 2008, Pages 857-864

In vivo measurement of internal and global macromolecular motions in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN;

EID: 47749148081     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.124420     Document Type: Article
Times cited : (56)

References (37)
  • 1
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure, and thermodynamics
    • Brooks, C. L., M. Karplus, and B. M. Pettitt. 1988. Proteins: a theoretical perspective of dynamics, structure, and thermodynamics. Adv. Chem. Phys. 71:1-249.
    • (1988) Adv. Chem. Phys , vol.71 , pp. 1-249
    • Brooks, C.L.1    Karplus, M.2    Pettitt, B.M.3
  • 3
    • 13844296720 scopus 로고    scopus 로고
    • A systems biology perspective on protein structural dynamics and signal tranduction
    • Rousseau, F., and J. Schymkowitz. 2005. A systems biology perspective on protein structural dynamics and signal tranduction. Curr. Opin. Struct. Biol. 15:23-30.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 23-30
    • Rousseau, F.1    Schymkowitz, J.2
  • 4
    • 4344642067 scopus 로고    scopus 로고
    • Protein motions promote catalysis
    • Tousignant, A., and J. N. Pelletier. 2004. Protein motions promote catalysis. Chem. Biol. 11:1037-1042.
    • (2004) Chem. Biol , vol.11 , pp. 1037-1042
    • Tousignant, A.1    Pelletier, J.N.2
  • 5
  • 8
    • 0025938315 scopus 로고
    • Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments
    • Smith, J. C. 1991. Protein dynamics: comparison of simulations with inelastic neutron scattering experiments. Q. Rev. Biophys. 24:227-291.
    • (1991) Q. Rev. Biophys , vol.24 , pp. 227-291
    • Smith, J.C.1
  • 9
    • 0029061330 scopus 로고
    • Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering
    • Andreani, C., A. Filabozzi, F. Menzinger, A. Desideri, A. Deriu, and D. Di Cola. 1995. Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering. Biophys. J. 68:2519-2523.
    • (1995) Biophys. J , vol.68 , pp. 2519-2523
    • Andreani, C.1    Filabozzi, A.2    Menzinger, F.3    Desideri, A.4    Deriu, A.5    Di Cola, D.6
  • 11
    • 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
  • 12
    • 0033064923 scopus 로고    scopus 로고
    • The temperature dependence of internal molecular motions 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 motions 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
  • 13
    • 0042266782 scopus 로고    scopus 로고
    • Protein dynamics on the picosecond timescale as affected by the environment: A quasielastic neutron scattering study
    • Paciaroni, A., A. Orecchini, S. Cinelli, G. Onori, R. E. Lechner, and J. Pieper. 2003. Protein dynamics on the picosecond timescale as affected by the environment: a quasielastic neutron scattering study. Chem. Phys. 292:397-404.
    • (2003) Chem. Phys , vol.292 , pp. 397-404
    • Paciaroni, A.1    Orecchini, A.2    Cinelli, S.3    Onori, G.4    Lechner, R.E.5    Pieper, J.6
  • 15
    • 0031548675 scopus 로고    scopus 로고
    • Dynamics of a globular protein as studied by neutron scattering and solid-state NMR
    • Zanotti, J. M., M. C. Bellissent-Funel, and J. Parello. 1997. Dynamics of a globular protein as studied by neutron scattering and solid-state NMR. Physica B (Amsterdam). 234:228-230.
    • (1997) Physica B (Amsterdam) , vol.234 , pp. 228-230
    • Zanotti, J.M.1    Bellissent-Funel, M.C.2    Parello, J.3
  • 16
    • 0043194670 scopus 로고    scopus 로고
    • Evolution of the internal dynamics of two globular proteins from dry powder to solution
    • Pérez, 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
    • Pérez, J.1    Zanotti, J.M.2    Durand, D.3
  • 17
    • 0031712270 scopus 로고    scopus 로고
    • Molecular motions and hydration of purple membranes and disk membranes studied by neutron scattering
    • Fitter, J., O. P. Ernst, T. Hauß, R. E. Lechner, K. P. Hofmann, and N. A. Dencher. 1998. Molecular motions and hydration of purple membranes and disk membranes studied by neutron scattering. Eur. Biophys. J. 27:638-645.
    • (1998) Eur. Biophys. J , vol.27 , pp. 638-645
    • Fitter, J.1    Ernst, O.P.2    Hauß, T.3    Lechner, R.E.4    Hofmann, K.P.5    Dencher, N.A.6
  • 18
    • 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
  • 19
    • 0030217736 scopus 로고    scopus 로고
    • Temperature dependence of molecular motions in the membrane protein bacteriorhodopsin from QINS
    • Fitter, J., R. E. Lechner, G. Büldt, and N. A. Dencher. 1996. Temperature dependence of molecular motions in the membrane protein bacteriorhodopsin from QINS. Physica B (Amsterdam). 226:61-65.
    • (1996) Physica B (Amsterdam) , vol.226 , pp. 61-65
    • Fitter, J.1    Lechner, R.E.2    Büldt, G.3    Dencher, N.A.4
  • 20
    • 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
  • 21
    • 0000265605 scopus 로고    scopus 로고
    • Interactions of hydration water and biological membranes studied by neutron scattering
    • Fitter, J., R. E. Lechner, and N. A. Dencher. 1999. Interactions of hydration water and biological membranes studied by neutron scattering. J. Phys. Chem. B. 103:8036-8050.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8036-8050
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 22
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis, R. J. 2001. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11:114-119.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 24
    • 0033991590 scopus 로고    scopus 로고
    • Cytoarchitecture and physical properties of cytoplasm: Volume, viscosity, diffusion, intracellular surface area
    • Luby-Phelps, K. 2000. Cytoarchitecture and physical properties of cytoplasm: volume, viscosity, diffusion, intracellular surface area. Int. Rev. Cytol. 192:189-221.
    • (2000) Int. Rev. Cytol , vol.192 , pp. 189-221
    • Luby-Phelps, K.1
  • 25
    • 34548254432 scopus 로고    scopus 로고
    • Microscopic diffusion and hydrodynamic interactions of hemoglobin in red blood cells
    • Doster, W., and S. Longeville. 2007. Microscopic diffusion and hydrodynamic interactions of hemoglobin in red blood cells. Biophys. J. 93:1360-1368.
    • (2007) Biophys. J , vol.93 , pp. 1360-1368
    • Doster, W.1    Longeville, S.2
  • 26
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis, R. J. 2001. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26:597-604.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 30
    • 1242343625 scopus 로고    scopus 로고
    • Tehei, M., B. Franzetti, D. Madern, M. Ginzburg, B. Z. Ginzburg, M. T. Giudici-Orticoni, M. Bruschi, and G. Zaccai. 2004. Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering. EMBO Rep. 5:66-70.
    • Tehei, M., B. Franzetti, D. Madern, M. Ginzburg, B. Z. Ginzburg, M. T. Giudici-Orticoni, M. Bruschi, and G. Zaccai. 2004. Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering. EMBO Rep. 5:66-70.
  • 32
    • 85031364740 scopus 로고    scopus 로고
    • Busch, S., W. Doster, S. Longeville, and V. G. Sakai. 2007. Microscopic protein diffusion at high concentration. MRS Bulletin. Quasi-elastic Neutron Scattering Conference 2006, p.117-116.
    • Busch, S., W. Doster, S. Longeville, and V. G. Sakai. 2007. Microscopic protein diffusion at high concentration. MRS Bulletin. Quasi-elastic Neutron Scattering Conference 2006, p.117-116.
  • 33
    • 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
  • 34
    • 33646083441 scopus 로고    scopus 로고
    • Influence of pressure on structure and dynamics of bovine pancreatic trypsin inhibitor (BPTI): Small angle and quasi-elastic neutron scattering studies
    • Appavou, M. S., G. Gibrat, and M. C. Bellissent-Funel. 2006. Influence of pressure on structure and dynamics of bovine pancreatic trypsin inhibitor (BPTI): small angle and quasi-elastic neutron scattering studies. Biochim. Biophys. Acta. 1764:414-423.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 414-423
    • Appavou, M.S.1    Gibrat, G.2    Bellissent-Funel, M.C.3
  • 35
    • 33646254850 scopus 로고    scopus 로고
    • Dynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scattering
    • Tehei, M., J. C. Smith, C. Monk, J. Ollivier, M. Oettl, V. Kurkal, J. L. Finney, and R. M. Daniel. 2006. Dynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scattering. Biophys. J. 90:1090-1097.
    • (2006) Biophys. J , vol.90 , pp. 1090-1097
    • Tehei, M.1    Smith, J.C.2    Monk, C.3    Ollivier, J.4    Oettl, M.5    Kurkal, V.6    Finney, J.L.7    Daniel, R.M.8
  • 37
    • 0038350006 scopus 로고    scopus 로고
    • The high-flux backscattering spectrometer at the NIST Center for Neutron Research
    • Meyer, A., R. M. Dimeo, P. M. Gehring, and D. A. Neumann. 2003. The high-flux backscattering spectrometer at the NIST Center for Neutron Research. Rev. Sci. Instrum. 74:2759-2777.
    • (2003) Rev. Sci. Instrum , vol.74 , pp. 2759-2777
    • Meyer, A.1    Dimeo, R.M.2    Gehring, P.M.3    Neumann, D.A.4


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