메뉴 건너뛰기




Volumn 76, Issue 2, 1999, Pages 1043-1047

Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYMYOGLOBIN; TREHALOSE;

EID: 0033051987     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77269-3     Document Type: Article
Times cited : (213)

References (26)
  • 1
    • 0001566390 scopus 로고
    • Novel carbohydrate metabolism in the resurrection plant Craterostigma plantagineum
    • Bianchi, G., A. Gamba, C. Murellie, F. Salamini, and D. Bertels. 1991. Novel carbohydrate metabolism in the resurrection plant Craterostigma plantagineum. Plant J. 1:355-359.
    • (1991) Plant J. , vol.1 , pp. 355-359
    • Bianchi, G.1    Gamba, A.2    Murellie, C.3    Salamini, F.4    Bertels, D.5
  • 2
    • 0031889847 scopus 로고    scopus 로고
    • A reduction of protein specific motions in CO-ligated myoglobin embedded in a trehalose glass
    • Cordone, L., P. Galajda, E. Vitrano, A. Gassmann, A. Ostermann, and F. Parak. 1998. A reduction of protein specific motions in CO-ligated myoglobin embedded in a trehalose glass. Eur. Biophys. J. 27:173-176.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 173-176
    • Cordone, L.1    Galajda, P.2    Vitrano, E.3    Gassmann, A.4    Ostermann, A.5    Parak, F.6
  • 3
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: The role of trehalose
    • Crowe, J. H., and L. M. Crowe. 1984. Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science. 223:701-703.
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2
  • 4
    • 0028922168 scopus 로고
    • Low temperature optical absorption spectroscopy: An approach to the study of stereodynamic properties of hemeproteins
    • Cupane, A., M. Leone, E. Vitrano, and L. Cordone 1995. Low temperature optical absorption spectroscopy: an approach to the study of stereodynamic properties of hemeproteins. Eur. Biophys. J. 23:385-398.
    • (1995) Eur. Biophys. J. , vol.23 , pp. 385-398
    • Cupane, A.1    Leone, M.2    Vitrano, E.3    Cordone, L.4
  • 5
    • 0025333959 scopus 로고
    • Temperature dependence of the low-frequency dynamics of myoglobin. Measurement of the vibrational frequency distribution by inelastic neutron scattering
    • Cusack, S., and W. Doster. 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 , pp. 243-251
    • Cusack, S.1    Doster, W.2
  • 6
    • 0026700192 scopus 로고
    • Protein dynamics: Vibrational coupling, spectral broadening mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape
    • Di Pace, A., A. Cupane, M. Leone, E. Vitrano, and L. Cordone. 1992. Protein dynamics: vibrational coupling, spectral broadening mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape. Biophys. J. 63:475-484.
    • (1992) Biophys. J. , vol.63 , pp. 475-484
    • Di Pace, A.1    Cupane, A.2    Leone, M.3    Vitrano, E.4    Cordone, L.5
  • 7
    • 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
  • 8
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: 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 membranes: 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
  • 11
    • 0029647450 scopus 로고
    • Protein reaction kinetics in a room-temperature glass
    • Hagen, S. J., J. Hofrichter, and W. A. Eaton. 1995. Protein reaction kinetics in a room-temperature glass. Science. 269:959-962.
    • (1995) Science , vol.269 , pp. 959-962
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 12
    • 0030197743 scopus 로고    scopus 로고
    • Germinate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature
    • Hagen, S. J., J. Hofrichter, and W. A. Eaton. 1996. Germinate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature. J. Phys. Chem. 100:12008-12021.
    • (1996) J. Phys. Chem. , vol.100 , pp. 12008-12021
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 13
    • 0028575357 scopus 로고
    • Thermal broadening of Soret band in heme complexes and in heme-proteins: Role of the iron dynamics
    • Leone, M., A. Cupane, V. Militello, and L. Cordone. 1994. Thermal broadening of Soret band in heme complexes and in heme-proteins: role of the iron dynamics. Eur. Biophys. J. 23:349-352.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 349-352
    • Leone, M.1    Cupane, A.2    Militello, V.3    Cordone, L.4
  • 14
    • 0028838470 scopus 로고
    • Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying
    • Leslie, S. B., E. Israeli, B. Lighthart, J. H. Crowe, and L. M. Crowe. 1995. Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying. Appl. Environ. Microbiol. 91:3592-3597.
    • (1995) Appl. Environ. Microbiol. , vol.91 , pp. 3592-3597
    • Leslie, S.B.1    Israeli, E.2    Lighthart, B.3    Crowe, J.H.4    Crowe, L.M.5
  • 16
    • 0030004479 scopus 로고    scopus 로고
    • Structural fluctuations of myoglobin from normal modes, Mössbauer, Raman, and absorption spectroscopy
    • Melkers, B., E. W. Knapp, F. Parak, L. Cordone, A. Cupane, and M. Leone. 1996. Structural fluctuations of myoglobin from normal modes, Mössbauer, Raman, and absorption spectroscopy. Biophys. J. 70: 2092-2099.
    • (1996) Biophys. J. , vol.70 , pp. 2092-2099
    • Melkers, B.1    Knapp, E.W.2    Parak, F.3    Cordone, L.4    Cupane, A.5    Leone, M.6
  • 17
    • 0029242120 scopus 로고
    • Trehalose metabolism-new horizons in technological applications
    • Panek, A. D. 1995. Trehalose metabolism-new horizons in technological applications. Braz. J. Med. Biol. Res. 28:169-181.
    • (1995) Braz. J. Med. Biol. Res. , vol.28 , pp. 169-181
    • Panek, A.D.1
  • 18
    • 0020333863 scopus 로고
    • Protein dynamics. Mossbauer spectroscopy on deoxymyoglobin crystals
    • Parak, F., E. W. Knapp, and D. Kucheida. 1982. Protein dynamics. Mossbauer spectroscopy on deoxymyoglobin crystals. J. Mol. Biol. 161:177-194.
    • (1982) J. Mol. Biol. , vol.161 , pp. 177-194
    • Parak, F.1    Knapp, E.W.2    Kucheida, D.3
  • 20
    • 0002943198 scopus 로고    scopus 로고
    • Functional dynamics in purple membrane
    • S. Cusack, H. Büttner, M. Ferrand, P. Langan, and P. Timmins, editors. Adenine Press, New York
    • Réat, V., G. Zaccai, M. Ferrand, and C. Pfister. 1997. Functional dynamics in purple membrane. In Biological Macromolecular Dynamics. S. Cusack, H. Büttner, M. Ferrand, P. Langan, and P. Timmins, editors. Adenine Press, New York. 117-122.
    • (1997) Biological Macromolecular Dynamics , pp. 117-122
    • Réat, V.1    Zaccai, G.2    Ferrand, M.3    Pfister, C.4
  • 22
    • 85030357018 scopus 로고
    • Institut Laue Langevin (Grenoble). Internal Report
    • Rieutord, F. 1991. Institut Laue Langevin (Grenoble). Internal Report.
    • (1991)
    • Rieutord, F.1
  • 23
    • 0002700870 scopus 로고    scopus 로고
    • Iterative calculation of the vibrational density of states from incoherent neutron scattering data with the account of double scattering
    • S. Cusack, H. Bhttner, M. Ferrand, P. Langan, and P. Timmins, editors. Adenine Press, New York
    • Settles, M., and W. Doster. 1997. Iterative calculation of the vibrational density of states from incoherent neutron scattering data with the account of double scattering. In Biological Macromolecular Dynamics. S. Cusack, H. Bhttner, M. Ferrand, P. Langan, and P. Timmins, editors. Adenine Press, New York. 3-8.
    • (1997) Biological Macromolecular Dynamics , pp. 3-8
    • Settles, M.1    Doster, W.2
  • 24
    • 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
  • 25
    • 0000473545 scopus 로고
    • The effects of environments and hydration on protein dynamics: A simulation study of myoglobin
    • Steinbach, P. J., R. J. Loncharich, and B. R. Brooks. 1991. The effects of environments and hydration on protein dynamics: a simulation study of myoglobin. Chem. Phys. 158:384-394.
    • (1991) Chem. Phys. , vol.158 , pp. 384-394
    • Steinbach, P.J.1    Loncharich, R.J.2    Brooks, B.R.3
  • 26
    • 0028922247 scopus 로고
    • Protective effect of disaccharides on restriction endonucleases during drying under vacuum
    • Uritani, M., M. Takai, and K. Yoshinaga. 1995. Protective effect of disaccharides on restriction endonucleases during drying under vacuum. J. Biochem. 117:774-779.
    • (1995) J. Biochem. , vol.117 , pp. 774-779
    • Uritani, M.1    Takai, M.2    Yoshinaga, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.