메뉴 건너뛰기




Volumn 76, Issue 5, 1999, Pages 2727-2734

Dehydration and crystallization of trehalose and sucrose glasses containing carbonmonoxy-myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; CARBON MONOXIDE; MYOGLOBIN; SUCROSE; TREHALOSE;

EID: 0033032336     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77425-4     Document Type: Article
Times cited : (43)

References (32)
  • 1
    • 0001644165 scopus 로고
    • The crystallization of hydrates from amorphous carbohydrates
    • Aldous, B. J., A. D. Auffret, and F. Franks. 1995. The crystallization of hydrates from amorphous carbohydrates. Cryo-letters 16:181-186.
    • (1995) Cryo-letters , vol.16 , pp. 181-186
    • Aldous, B.J.1    Auffret, A.D.2    Franks, F.3
  • 4
    • 0020577970 scopus 로고
    • Multiple internal reflectance infrared spectra of variably hydrated hemoglobin and myoglobin films: Effects of globin hydration on ligand conformer dynamics and reactivity at the heme
    • Brown, W. E., J. W. Sutcliff, and P. D. Pulsinelli. 1983. Multiple internal reflectance infrared spectra of variably hydrated hemoglobin and myoglobin films: effects of globin hydration on ligand conformer dynamics and reactivity at the heme. Biochemistry. 22:2914-2923.
    • (1983) Biochemistry , vol.22 , pp. 2914-2923
    • Brown, W.E.1    Sutcliff, J.W.2    Pulsinelli, P.D.3
  • 5
    • 0019569337 scopus 로고
    • Dynamic protein structures: Infrared evidence for four discrete rapidly interconverting conformers at the carbon monoxide binding site of bovine heart myoglobin
    • Caughey, W. S., H. Shimada, G. C. Miles, and M. P. Tucker. 1981. Dynamic protein structures: infrared evidence for four discrete rapidly interconverting conformers at the carbon monoxide binding site of bovine heart myoglobin. Proc. Natl. Acad. Sci. USA. 78:2903-2907.
    • (1981) Proc. Natl. Acad. Sci. USA. , vol.78 , pp. 2903-2907
    • Caughey, W.S.1    Shimada, H.2    Miles, G.C.3    Tucker, M.P.4
  • 6
    • 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
  • 7
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbonmonoxy-myoglobin at high temperature
    • Cordone, L., M. Ferrand, E. Vitrano, and G. Zaccai. 1999. Harmonic behavior of trehalose-coated carbonmonoxy-myoglobin at high temperature. Biophys. J. 76:000-000.
    • (1999) Biophys. J. , vol.76 , pp. 000-000
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 8
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe, L. M., D. S. Reid, and J. H. Crowe. 1996. Is trehalose special for preserving dry biomaterials? Biophys. J. 71:2087-2093.
    • (1996) Biophys. J. , vol.71 , pp. 2087-2093
    • Crowe, L.M.1    Reid, D.S.2    Crowe, J.H.3
  • 9
    • 0026700192 scopus 로고
    • 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. 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
  • 10
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • Doster, W., S. Cusack, and W. Perry. 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    Perry, W.3
  • 14
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 15
    • 0021818674 scopus 로고
    • Structure, dynamics and reactivity in hemoglobin
    • Friedman, J. M. 1985. Structure, dynamics and reactivity in hemoglobin. Science. 228:1273-1280.
    • (1985) Science , vol.228 , pp. 1273-1280
    • Friedman, J.M.1
  • 17
    • 33845184276 scopus 로고
    • Phase relations and vitrification in saccharide-water solutions and trehalose anomaly
    • Green, J. L., and C. A. Angell. 1989. Phase relations and vitrification in saccharide-water solutions and trehalose anomaly. J. Phys. Chem. 93: 2880-2882.
    • (1989) J. Phys. Chem. , vol.93 , pp. 2880-2882
    • Green, J.L.1    Angell, C.A.2
  • 18
    • 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
  • 19
    • 0030197743 scopus 로고    scopus 로고
    • Geminate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature
    • Hagen, S. J., J. Hofrichter, and W. A. Eaton. 1996. Geminate 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
  • 20
    • 0032512436 scopus 로고    scopus 로고
    • Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin
    • Kleinert, T., W. Doster, H. Leyser, W. Petry, V. Schwarz, and M. Settles. 1998. Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin. Biochemistry. 37:717-733.
    • (1998) Biochemistry , vol.37 , pp. 717-733
    • Kleinert, T.1    Doster, W.2    Leyser, H.3    Petry, W.4    Schwarz, V.5    Settles, M.6
  • 21
    • 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
  • 23
    • 0028094598 scopus 로고
    • FTIR spectroscopic study of the dynamics of conformational substates in hydrated carbonyl-myoglobin films via temperature dependence of the CO stretching band parameters
    • Mayer, E. 1994. FTIR spectroscopic study of the dynamics of conformational substates in hydrated carbonyl-myoglobin films via temperature dependence of the CO stretching band parameters. Biophys. J. 67: 862-873.
    • (1994) Biophys. J. , vol.67 , pp. 862-873
    • Mayer, E.1
  • 24
    • 0030004479 scopus 로고    scopus 로고
    • Structural fluctuations of myoglobin from normal modes, Mössbauer, Raman, and absorption spectroscopy
    • Melchers, 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
    • Melchers, B.1    Knapp, E.W.2    Parak, F.3    Cordone, L.4    Cupane, A.5    Leone, M.6
  • 25
    • 0024334934 scopus 로고
    • Resonance raman investigation of site-directed mutants of myoglobin: Effects of distal histidine replacement
    • Morikis, D., P. M. Champion, B. A. Springer, and S. G. Sligar. 1989. Resonance Raman investigation of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry. 28:4791-4800.
    • (1989) Biochemistry , vol.28 , pp. 4791-4800
    • Morikis, D.1    Champion, P.M.2    Springer, B.A.3    Sligar, S.G.4
  • 28
    • 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
  • 30
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibitions by stabilizers
    • Prestrelski, S. J., N. Tedeschi, T. Arakawa, and J. F. Carpenter. 1993. Dehydration-induced conformational transitions in proteins and their inhibitions by stabilizers. Biophys. J. 65:661-671.
    • (1993) Biophys. J. , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 31
    • 0030921074 scopus 로고    scopus 로고
    • Trehalose prevents myoglobin collapse and preserves its internal mobility
    • Sastry, G. M., and N. Agmon. 1997. Trehalose prevents myoglobin collapse and preserves its internal mobility. Biochemistry. 36:7097-7108.
    • (1997) Biochemistry , vol.36 , pp. 7097-7108
    • Sastry, G.M.1    Agmon, N.2
  • 32
    • 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.