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Volumn 1749, Issue 2, 2005, Pages 252-281

Internal dynamics and protein-matrix coupling in trehalose-coated proteins

Author keywords

Carboxy myoglobin; CO stretching band; Flash photolysis; Reaction centre; Trehalose; Water association band

Indexed keywords

CARBON MONOXIDE; HEME; HYDROGEN; MEMBRANE PROTEIN; MYOGLOBIN; PROTEIN; SOLVENT; SUCROSE; TREHALOSE; WATER;

EID: 20144372629     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.03.004     Document Type: Review
Times cited : (122)

References (189)
  • 3
    • 0344984273 scopus 로고    scopus 로고
    • Coupling between the thermal evolution of the heme pocket and the external matrix structure in trehalose coated carboxymyoglobin
    • S. Giuffrida, G. Cottone, F. Librizzi, and L. Cordone Coupling between the thermal evolution of the heme pocket and the external matrix structure in trehalose coated carboxymyoglobin J. Phys. Chem., B 107 2003 13211 13217
    • (2003) J. Phys. Chem., B , vol.107 , pp. 13211-13217
    • Giuffrida, S.1    Cottone, G.2    Librizzi, F.3    Cordone, L.4
  • 5
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • H. Frauenfelder, S.G. Sligar, and P.G. Wolynes The energy landscapes and motions of proteins Science 254 1991 1598 1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 6
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • H. Frauenfelder, B.H. McMahon, R.H. Austin, K. Chu, and J.T. Groves The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin Proc. Natl. Acad. Sci. U. S. A. 98 2001 2370 2374
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 7
    • 0346103676 scopus 로고    scopus 로고
    • Direct observation of tiers in the energy landscape of a chromoprotein: A single-molecule study
    • C. Hofmann, T.J. Aartsma, H. Michel, and J. Köhler Direct observation of tiers in the energy landscape of a chromoprotein: a single-molecule study Proc. Natl. Acad. Sci. U. S. A. 100 2003 15534 15538
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15534-15538
    • Hofmann, C.1    Aartsma, T.J.2    Michel, H.3    Köhler, J.4
  • 8
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • J.D. Bryngelson, and P.J. Wolynes Spin glasses and the statistical mechanics of protein folding Proc. Natl. Acad. Sci. U. S. A. 84 1987 7524 7528
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.J.2
  • 9
    • 0023140044 scopus 로고
    • Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin
    • R. Elber, and M. Karplus Multiple conformational states of proteins: a molecular dynamics analysis of myoglobin Science 235 1987 318 321
    • (1987) Science , vol.235 , pp. 318-321
    • Elber, R.1    Karplus, M.2
  • 10
    • 0001595086 scopus 로고
    • Proteins and glasses: A relaxation study in the millikelvin range
    • J. Gafert, H. Pschierer, and J. Friedrich Proteins and glasses: a relaxation study in the millikelvin range Phys. Rev. Lett. 74 1995 3704 3707
    • (1995) Phys. Rev. Lett. , vol.74 , pp. 3704-3707
    • Gafert, J.1    Pschierer, H.2    Friedrich, J.3
  • 11
    • 0035250097 scopus 로고    scopus 로고
    • Effects of solvent viscosity on protein dynamics: Infrared vibrational echo experiments and theory
    • D. Rector, J. Jiang, M.A. Berg, and M.D. Fayer Effects of solvent viscosity on protein dynamics: infrared vibrational echo experiments and theory J. Phys. Chem., B 105 2001 1081 1092
    • (2001) J. Phys. Chem., B , vol.105 , pp. 1081-1092
    • Rector, D.1    Jiang, J.2    Berg, M.A.3    Fayer, M.D.4
  • 12
    • 0034808210 scopus 로고    scopus 로고
    • Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes
    • M. Weik, R.B.G. Ravelli, I. Silman, J.L. Sussman, P. Gros, and J. Kroon Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes Protein Sci. 10 2001 1953 1961
    • (2001) Protein Sci. , vol.10 , pp. 1953-1961
    • Weik, M.1    Ravelli, R.B.G.2    Silman, I.3    Sussman, J.L.4    Gros, P.5    Kroon, J.6
  • 13
    • 0037080694 scopus 로고    scopus 로고
    • Residual water modulates the dynamics of the protein and of the external matrix in "trehalose coated" MbCO: An infrared and flash photolysis study
    • F. Librizzi, C. Viappiani, S. Abbruzzetti, and L. Cordone Residual water modulates the dynamics of the protein and of the external matrix in "trehalose coated" MbCO: an infrared and flash photolysis study J. Chem. Phys. 116 2002 1193 1200
    • (2002) J. Chem. Phys. , vol.116 , pp. 1193-1200
    • Librizzi, F.1    Viappiani, C.2    Abbruzzetti, S.3    Cordone, L.4
  • 14
    • 0036156512 scopus 로고    scopus 로고
    • Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: Trapping of conformational substates at room temperature
    • G. Palazzo, A. Mallardi, A. Hochkoeppler, L. Cordone, and G. Venturoli Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: trapping of conformational substates at room temperature Biophys. J. 82 2002 558 568
    • (2002) Biophys. J. , vol.82 , pp. 558-568
    • Palazzo, G.1    Mallardi, A.2    Hochkoeppler, A.3    Cordone, L.4    Venturoli, G.5
  • 15
    • 6344281045 scopus 로고    scopus 로고
    • Structure-dynamics coupling between protein and external matrix in sucrose coated and in trehalose coated MbCO: A FTIR study
    • S. Giuffrida, G. Cottone, and L. Cordone Structure-dynamics coupling between protein and external matrix in sucrose coated and in trehalose coated MbCO: a FTIR study J. Phys. Chem., B 108 2004 15415 15421
    • (2004) J. Phys. Chem., B , vol.108 , pp. 15415-15421
    • Giuffrida, S.1    Cottone, G.2    Cordone, L.3
  • 16
    • 0032512436 scopus 로고    scopus 로고
    • Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin
    • T. Kleinert, W. Doster, H. Leyser, W. Petry, V. Schwarz, and M. Settles Solvent composition and viscosity effects on the kinetics of CO binding to horse myoglobin Biochemistry 37 1998 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
  • 17
    • 0036733803 scopus 로고    scopus 로고
    • Solvent effect on conformational dynamics of proteins: Cytocrome C in a dried trehalose film
    • V.V. Ponkratov, J. Friedrich, and J.M. Vanderkooi Solvent effect on conformational dynamics of proteins: cytocrome C in a dried trehalose film J. Chem. Phys. 117 2002 4594 4601
    • (2002) J. Chem. Phys. , vol.117 , pp. 4594-4601
    • Ponkratov, V.V.1    Friedrich, J.2    Vanderkooi, J.M.3
  • 18
    • 0020333863 scopus 로고
    • Protein dynamics: Mössbauer spectroscopy on deoxymyoglobin crystals
    • F. Parak, E.W. Knapp, and D. Kucheida Protein dynamics: Mössbauer spectroscopy on deoxymyoglobin crystals J. Mol. Biol. 161 1982 177 194
    • (1982) J. Mol. Biol. , vol.161 , pp. 177-194
    • Parak, F.1    Knapp, E.W.2    Kucheida, D.3
  • 19
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • W. Doster, S. Cusak, and W. Petry Dynamical transition of myoglobin revealed by inelastic neutron scattering Nature 337 1989 754 756
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusak, S.2    Petry, W.3
  • 21
    • 0029061330 scopus 로고
    • Dynamics of hydrogen atoms in superoxide dismutase by quasi elastic neutron scattering
    • C. Andreani, A. Filabozzi, F. Menzinger, A. Desideri, A. Deriu, and D. Di Cola Dynamics of hydrogen atoms in superoxide dismutase by quasi elastic neutron scattering Biophys. J. 68 1995 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
  • 22
    • 0033064923 scopus 로고    scopus 로고
    • The temperature dependence of internal molecular motions in hydrated and dry alpha-amylase: The role of hydration water in the dynamical transition of proteins
    • J. Fitter The temperature dependence of internal molecular motions in hydrated and dry alpha-amylase: the role of hydration water in the dynamical transition of proteins Biophys. J. 76 1999 1042 1043
    • (1999) Biophys. J. , vol.76 , pp. 1042-1043
    • Fitter, J.1
  • 23
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the environment on the protein dynamical transition: A neutron scattering study
    • A. Paciaroni, S. Cinelli, and G. Onori Effect of the environment on the protein dynamical transition: a neutron scattering study Biophys. J. 83 2002 1157 1164
    • (2002) Biophys. J. , vol.83 , pp. 1157-1164
    • Paciaroni, A.1    Cinelli, S.2    Onori, G.3
  • 24
    • 0025008125 scopus 로고
    • The temperature dependence of hydrated myoglobin: Comparison of force field calculations with neutron scattering
    • R.J. Loncharich, and B.R. Brooks The temperature dependence of hydrated myoglobin: comparison of force field calculations with neutron scattering J. Mol. Biol. 215 1990 439 455
    • (1990) J. Mol. Biol. , vol.215 , pp. 439-455
    • Loncharich, R.J.1    Brooks, B.R.2
  • 25
    • 0000473545 scopus 로고
    • The effects of environment and hydration on protein dynamics: A simulation study of myoglobin
    • P.J. Steinbach, R.J. Loncharich, and B.R. Brooks The effects of environment and hydration on protein dynamics: a simulation study of myoglobin Chem. Phys. 158 1991 383 394
    • (1991) Chem. Phys. , vol.158 , pp. 383-394
    • Steinbach, P.J.1    Loncharich, R.J.2    Brooks, B.R.3
  • 27
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • A. Ansari, C.M. Jones, E.R. Henry, J. Hofrichter, and W. Eaton The role of solvent viscosity in the dynamics of protein conformational changes Science 256 1992 1796 1798
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.5
  • 30
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms
    • J.H. Crowe, and L.M. Crowe Preservation of membranes in anhydrobiotic organisms Science 223 1984 701 703
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2
  • 31
    • 0001566390 scopus 로고
    • Novel carbohydrate metabolism in the resurrection plant Craterostigma plantagineum
    • G. Bianchi, A. Gamba, C. Murellie, F. Salamini, and D. Bartels Novel carbohydrate metabolism in the resurrection plant Craterostigma plantagineum Plant J. 1 1991 355 359
    • (1991) Plant J. , vol.1 , pp. 355-359
    • Bianchi, G.1    Gamba, A.2    Murellie, C.3    Salamini, F.4    Bartels, D.5
  • 32
    • 0029242120 scopus 로고
    • Trehalose metabolism-new horizons in technological applications
    • A.D. Panek Trehalose metabolism-new horizons in technological applications Braz. J. Med. Biol. Res. 28 1995 169 181
    • (1995) Braz. J. Med. Biol. Res. , vol.28 , pp. 169-181
    • Panek, A.D.1
  • 33
    • 0007995991 scopus 로고
    • Freeze-dried lyposomes
    • F. Puisieux P. Covreur L. Delattre J.P. Devissaguet Editions de Santé Paris
    • L.M. Crowe, and J.H. Crowe Freeze-dried lyposomes F. Puisieux P. Covreur L. Delattre J.P. Devissaguet Liposomes, New Systems and New Trends in their Applications 1995 Editions de Santé Paris 237 272
    • (1995) Liposomes, New Systems and New Trends in Their Applications , pp. 237-272
    • Crowe, L.M.1    Crowe, J.H.2
  • 34
    • 0036182386 scopus 로고    scopus 로고
    • Lesson from nature: A role of sugars in anhydrobiosis
    • L.M. Crowe Lesson from nature: a role of sugars in anhydrobiosis Comp. Biochem. Physiol., A 132 2002 505 513
    • (2002) Comp. Biochem. Physiol., a , vol.132 , pp. 505-513
    • Crowe, L.M.1
  • 35
    • 0029647450 scopus 로고
    • Protein reaction kinetics in a room-temperature glass
    • S.J. Hagen, J. Hofrichter, and W.A. Eaton Protein reaction kinetics in a room-temperature glass Science 269 1995 959 962
    • (1995) Science , vol.269 , pp. 959-962
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 36
    • 0030197743 scopus 로고    scopus 로고
    • Geminate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature
    • S.J. Hagen, J. Hofrichter, and W.A. Eaton Geminate rebinding and conformational dynamics of myoglobin embedded in a glass at room temperature J. Phys. Chem. 100 1996 12008 12021
    • (1996) J. Phys. Chem. , vol.100 , pp. 12008-12021
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 37
    • 0036298976 scopus 로고    scopus 로고
    • Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories
    • D. Dantsker, U. Samuni, A.J. Friedman, M. Yang, A. Ray, and J.M. Friedman Geminate rebinding in trehalose-glass embedded myoglobins reveals residue-specific control of intramolecular trajectories J. Mol. Biol. 315 2002 239 251
    • (2002) J. Mol. Biol. , vol.315 , pp. 239-251
    • Dantsker, D.1    Samuni, U.2    Friedman, A.J.3    Yang, M.4    Ray, A.5    Friedman, J.M.6
  • 39
    • 0031889847 scopus 로고    scopus 로고
    • A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass
    • L. Cordone, P. Galajda, E. Vitrano, A. Gassmann, A. Ostermann, and F. Parak A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass Eur. Biophys. J. 27 1998 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
  • 40
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    • L. Cordone, M. Ferrand, E. Vitrano, and G. Zaccai Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature Biophys. J. 76 1999 1043 1047
    • (1999) Biophys. J. , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 42
    • 0035144443 scopus 로고    scopus 로고
    • Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix
    • G. Cottone, L. Cordone, and G. Ciccotti Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix Biophys. J. 80 2001 931 938
    • (2001) Biophys. J. , vol.80 , pp. 931-938
    • Cottone, G.1    Cordone, L.2    Ciccotti, G.3
  • 43
    • 0001633441 scopus 로고    scopus 로고
    • Biomolecules: Fluctuations and relaxations
    • H. Frauenfelder G. Hummer R. Garcia AIP American Institute of Physics Melville, NY
    • F. Parak, A. Ostermann, A. Gassmann, C. Scherk, S.H. Chong, A. Kidera, and N. Go Biomolecules: fluctuations and relaxations H. Frauenfelder G. Hummer R. Garcia Biological Physics 1999 AIP American Institute of Physics Melville, NY 117 127
    • (1999) Biological Physics , pp. 117-127
    • Parak, F.1    Ostermann, A.2    Gassmann, A.3    Scherk, C.4    Chong, S.H.5    Kidera, A.6    Go, N.7
  • 44
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interaction of carbohydrates with dried proteins
    • J.F. Carpenter, and J.H. Crowe An infrared spectroscopic study of the interaction of carbohydrates with dried proteins Biochemistry 28 1989 3916 3922
    • (1989) Biochemistry , vol.28 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 45
    • 0028151971 scopus 로고
    • IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lisozyme
    • P.S. Belton, and A.M. Gil IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lisozyme Biopolymers 34 1994 957 961
    • (1994) Biopolymers , vol.34 , pp. 957-961
    • Belton, P.S.1    Gil, A.M.2
  • 46
    • 0842302347 scopus 로고    scopus 로고
    • Trehalose-enzyme interactions result in structure stabilization and activity inhibition
    • J.G. Sampedro, and S. Uribe Trehalose-enzyme interactions result in structure stabilization and activity inhibition Mol. Cell. Biochem. 256 2004 319 327
    • (2004) Mol. Cell. Biochem. , vol.256 , pp. 319-327
    • Sampedro, J.G.1    Uribe, S.2
  • 47
    • 33845184276 scopus 로고
    • Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly
    • J. Green, and C.A. Angell Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly J. Phys. Chem. 93 1989 2880 2882
    • (1989) J. Phys. Chem. , vol.93 , pp. 2880-2882
    • Green, J.1    Angell, C.A.2
  • 48
    • 0030983570 scopus 로고    scopus 로고
    • Molecular-dynamics study of aqueous solution of trehalose and maltose: Implication for the biological function of trehalose
    • M. Sakurai, M. Murata, Y. Inoue, A. Hino, and S. Kobayashi Molecular-dynamics study of aqueous solution of trehalose and maltose: implication for the biological function of trehalose Bull. Chem. Soc. Jpn. 70 1997 847 858
    • (1997) Bull. Chem. Soc. Jpn. , vol.70 , pp. 847-858
    • Sakurai, M.1    Murata, M.2    Inoue, Y.3    Hino, A.4    Kobayashi, S.5
  • 49
    • 33748668803 scopus 로고    scopus 로고
    • Water interaction with α,α-trehalose: Molecular dynamics simulation
    • G. Bonanno, R. Noto, and S.L. Fornili Water interaction with α,α-trehalose: molecular dynamics simulation J. Chem. Soc., Faraday Trans. 94 1998 2755 2762
    • (1998) J. Chem. Soc., Faraday Trans. , vol.94 , pp. 2755-2762
    • Bonanno, G.1    Noto, R.2    Fornili, S.L.3
  • 50
    • 0000531647 scopus 로고    scopus 로고
    • Computer simulation of the cryoprotectant disaccharide α,α-trehalose in aqueous solution
    • P.B. Conrad, and J.J. de Pablo Computer simulation of the cryoprotectant disaccharide α,α-trehalose in aqueous solution J. Phys. Chem., A 103 1999 4049 4055
    • (1999) J. Phys. Chem., a , vol.103 , pp. 4049-4055
    • Conrad, P.B.1    De Pablo, J.J.2
  • 51
    • 0034825494 scopus 로고    scopus 로고
    • Molecular simulation of sucrose solutions near the glass transition temperature
    • N.C. Ekdawi-Sever, P.B. Conrad, and J.J. de Pablo Molecular simulation of sucrose solutions near the glass transition temperature J. Phys. Chem., A 105 2001 734 742
    • (2001) J. Phys. Chem., a , vol.105 , pp. 734-742
    • Ekdawi-Sever, N.C.1    Conrad, P.B.2    De Pablo, J.J.3
  • 52
    • 2342427533 scopus 로고    scopus 로고
    • Mean-square displacement relationship in bioprotectant systems by elastic neutron scattering
    • S. Magazù, G. Maisano, P. Migliardo, and C. Mondelli Mean-square displacement relationship in bioprotectant systems by elastic neutron scattering Biophys. J. 86 2004 3241 3249
    • (2004) Biophys. J. , vol.86 , pp. 3241-3249
    • Magazù, S.1    Maisano, G.2    Migliardo, P.3    Mondelli, C.4
  • 53
    • 0037019460 scopus 로고    scopus 로고
    • Molecular dynamics of water at the protein-solvent interface
    • A.R. Bizzarri, and S. Cannistraro Molecular dynamics of water at the protein-solvent interface J. Phys. Chem., B 106 2002 6617 6633
    • (2002) J. Phys. Chem., B , vol.106 , pp. 6617-6633
    • Bizzarri, A.R.1    Cannistraro, S.2
  • 54
    • 0036902487 scopus 로고    scopus 로고
    • Protein-trehalose-water structures in trehalose coated carboxy myoglobin
    • G. Cottone, G. Ciccotti, and L. Cordone Protein-trehalose-water structures in trehalose coated carboxy myoglobin J. Chem. Phys. 117 2002 9862 9866
    • (2002) J. Chem. Phys. , vol.117 , pp. 9862-9866
    • Cottone, G.1    Ciccotti, G.2    Cordone, L.3
  • 55
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • G. Xie, and S.N. Timasheff The thermodynamic mechanism of protein stabilization by trehalose Biophys. Chem. 64 1997 25
    • (1997) Biophys. Chem. , vol.64 , pp. 25
    • Xie, G.1    Timasheff, S.N.2
  • 56
    • 1442300062 scopus 로고    scopus 로고
    • Trehalose-protein interaction in aqueous solution
    • R.D. Lins, C.S. Pereira, and P.H. Hunenberger Trehalose-protein interaction in aqueous solution Proteins 55 2004 177 186
    • (2004) Proteins , vol.55 , pp. 177-186
    • Lins, R.D.1    Pereira, C.S.2    Hunenberger, P.H.3
  • 57
    • 0242385390 scopus 로고    scopus 로고
    • Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides
    • A.K. Sum, R. Faller, and J.J. de Pablo Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides Biophys. J. 85 2003 2830 2844
    • (2003) Biophys. J. , vol.85 , pp. 2830-2844
    • Sum, A.K.1    Faller, R.2    De Pablo, J.J.3
  • 58
    • 1942519438 scopus 로고    scopus 로고
    • Interaction of the disaccharide trehalose with a phospholipid bilayer: A molecular dynamics study
    • C.S. Pereira, R.D. Lins, I. Chandrasekhar, L.C.G. Freitas, and P.H. Hunenberger Interaction of the disaccharide trehalose with a phospholipid bilayer: a molecular dynamics study Biophys. J. 86 2004 2273 2285
    • (2004) Biophys. J. , vol.86 , pp. 2273-2285
    • Pereira, C.S.1    Lins, R.D.2    Chandrasekhar, I.3    Freitas, L.C.G.4    Hunenberger, P.H.5
  • 59
    • 4444359475 scopus 로고    scopus 로고
    • Molecular dynamics simulation study of the interaction of trehalose with lipid membranes
    • M.A. Villarreal, S.B. Dyaz, E.A. Disalvo, and G.G. Montich Molecular dynamics simulation study of the interaction of trehalose with lipid membranes Langmuir 20 2004 7844 7851
    • (2004) Langmuir , vol.20 , pp. 7844-7851
    • Villarreal, M.A.1    Dyaz, S.B.2    Disalvo, E.A.3    Montich, G.G.4
  • 60
    • 0034537809 scopus 로고    scopus 로고
    • An investigation of the water binding properties of protein + sugar systems
    • E.C. Lopez-Diez, and S. Bone An investigation of the water binding properties of protein + sugar systems Phys. Med. Biol. 45 2000 3577 3588
    • (2000) Phys. Med. Biol. , vol.45 , pp. 3577-3588
    • Lopez-Diez, E.C.1    Bone, S.2
  • 62
    • 19044399611 scopus 로고    scopus 로고
    • Role of protein-water hydrogen bond dynamics in the protein dynamical transition
    • M. Tarek, and D.J. Tobias Role of protein-water hydrogen bond dynamics in the protein dynamical transition Phys. Rev. Lett. 88 2002 8101 8104
    • (2002) Phys. Rev. Lett. , vol.88 , pp. 8101-8104
    • Tarek, M.1    Tobias, D.J.2
  • 64
    • 3543046791 scopus 로고    scopus 로고
    • Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose amorphous matrices
    • F. Francia, G. Palazzo, A. Mallardi, L. Cordone, and G. Venturoli Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose amorphous matrices Biochim. Biophys. Acta, Bioenerg. 1658 2004 50 57
    • (2004) Biochim. Biophys. Acta, Bioenerg. , vol.1658 , pp. 50-57
    • Francia, F.1    Palazzo, G.2    Mallardi, A.3    Cordone, L.4    Venturoli, G.5
  • 68
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • J. Vojtěchovsky, K. Chu, J. Berendzen, R.M. Sweet, and I. Schlichting Crystal structures of myoglobin-ligand complexes at near-atomic resolution Biophys. J. 77 1999 2153 2174
    • (1999) Biophys. J. , vol.77 , pp. 2153-2174
    • Vojtěchovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet, R.M.4    Schlichting, I.5
  • 69
    • 0001341970 scopus 로고
    • A molecular model for the major conformational substates in heme proteins
    • E. Oldfield, K. Guo, J.D. Augspurger, and C.E. Dykstra A molecular model for the major conformational substates in heme proteins J. Am. Chem. Soc. 113 1991 7537 7541
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7537-7541
    • Oldfield, E.1    Guo, K.2    Augspurger, J.D.3    Dykstra, C.E.4
  • 70
    • 0030936852 scopus 로고    scopus 로고
    • Molecular dynamics simulation study of the B-states of solvated carbon monoxymyoglobin
    • J. Ma, S.S. Huo, and J.E. Straub Molecular dynamics simulation study of the B-states of solvated carbon monoxymyoglobin J. Am. Chem. Soc. 119 1997 2541 2551
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2541-2551
    • Ma, J.1    Huo, S.S.2    Straub, J.E.3
  • 71
    • 0031880931 scopus 로고    scopus 로고
    • Computer simulations of carbon monoxide photodissociation in myoglobin
    • J. Meller, and R. Eber Computer simulations of carbon monoxide photodissociation in myoglobin Biophys. J. 74 1998 789 802
    • (1998) Biophys. J. , vol.74 , pp. 789-802
    • Meller, J.1    Eber, R.2
  • 72
    • 0037032263 scopus 로고    scopus 로고
    • An electrostatic model for the frequency shifts in the carbonmonoxy stretching band of myoglobin: Correlation of hydrogen bonding and the Stark tuning rate
    • S. Franzen An electrostatic model for the frequency shifts in the carbonmonoxy stretching band of myoglobin: correlation of hydrogen bonding and the Stark tuning rate J. Am. Chem. Soc. 124 2002 13271 13281
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13271-13281
    • Franzen, S.1
  • 73
    • 2642588311 scopus 로고    scopus 로고
    • Vibrational stark effects on carbonyl, nitrile, and nitrosyl compounds including heme ligands, CO, CN, and NO, studied with density functional theory
    • S.D. Dalosto, J.M. Vanderkooi, and K.A. Sharp Vibrational stark effects on carbonyl, nitrile, and nitrosyl compounds including heme ligands, CO, CN, and NO, studied with density functional theory J. Phys. Chem. 108 2004 6540 6547
    • (2004) J. Phys. Chem. , vol.108 , pp. 6540-6547
    • Dalosto, S.D.1    Vanderkooi, J.M.2    Sharp, K.A.3
  • 74
    • 0028328331 scopus 로고
    • Structural determinant of the stretching frequency of CO bound to myoglobin
    • T. Li, M.L. Quillin, G.N. Phillips Jr., and J.S. Olson Structural determinant of the stretching frequency of CO bound to myoglobin Biochemistry 33 1994 1433 1446
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 75
    • 0035957233 scopus 로고    scopus 로고
    • Carbonmonoxy horseradish peroxidase as a function of pH and substrate: Influence of local electric fields on the optical and infrared spectra
    • A.D. Kaposi, W.W. Wright, J. Fidy, S.S. Stavrov, J.M. Vanderkooi, and I. Rasnik Carbonmonoxy horseradish peroxidase as a function of pH and substrate: influence of local electric fields on the optical and infrared spectra Biochemistry 40 2001 3483 3491
    • (2001) Biochemistry , vol.40 , pp. 3483-3491
    • Kaposi, A.D.1    Wright, W.W.2    Fidy, J.3    Stavrov, S.S.4    Vanderkooi, J.M.5    Rasnik, I.6
  • 76
    • 0035201709 scopus 로고    scopus 로고
    • Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase
    • A.D. Kaposi, J.M. Vanderkooi, W.W. Wright, J. Fidy, and S.S. Stavrov Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase Biophys. J. 81 2001 3472 3482
    • (2001) Biophys. J. , vol.81 , pp. 3472-3482
    • Kaposi, A.D.1    Vanderkooi, J.M.2    Wright, W.W.3    Fidy, J.4    Stavrov, S.S.5
  • 77
    • 0141739441 scopus 로고    scopus 로고
    • Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations
    • A.D. Kaposi, N.V. Prabhu, S.D. Dalosto, K.A. Sharp, W.W. Wright, S.S. Stavrov, and J.M. Vanderkooi Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations Biophys. Chem. 106 2003 1 14
    • (2003) Biophys. Chem. , vol.106 , pp. 1-14
    • Kaposi, A.D.1    Prabhu, N.V.2    Dalosto, S.D.3    Sharp, K.A.4    Wright, W.W.5    Stavrov, S.S.6    Vanderkooi, J.M.7
  • 79
    • 0001965163 scopus 로고    scopus 로고
    • Inhibition of a substates interconversion in trehalose coated carbonmonoxy-myoglobin
    • H. Frauenfelder G. Hummer R. Garcia AIP American Institute of Physics Melville, NY
    • F. Librizzi, E. Vitrano, and L. Cordone Inhibition of a substates interconversion in trehalose coated carbonmonoxy-myoglobin H. Frauenfelder G. Hummer R. Garcia Biological Physics 1999 AIP American Institute of Physics Melville, NY 132 138
    • (1999) Biological Physics , pp. 132-138
    • Librizzi, F.1    Vitrano, E.2    Cordone, L.3
  • 80
    • 0002055106 scopus 로고    scopus 로고
    • Spatially heterogeneous dynamics in supercooled liquids
    • M.D. Ediger Spatially heterogeneous dynamics in supercooled liquids Annu. Rev. Phys. Chem. 51 2000 99 128
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 99-128
    • Ediger, M.D.1
  • 82
    • 0033032336 scopus 로고    scopus 로고
    • Dehydration and crystallization of trehalose and sucrose glasses containing carbonmonoxy-myoglobin
    • F. Librizzi, E. Vitrano, and L. Cordone Dehydration and crystallization of trehalose and sucrose glasses containing carbonmonoxy-myoglobin Biophys. J. 76 1999 2727 2734
    • (1999) Biophys. J. , vol.76 , pp. 2727-2734
    • Librizzi, F.1    Vitrano, E.2    Cordone, L.3
  • 83
  • 85
    • 0030771840 scopus 로고    scopus 로고
    • Vibrational frequency shifts as a probe of hydrogen bonds: Thermal expansion and glass transition of myoglobin in mixed solvent
    • F. Demmel, W. Doster, W. Petry, and A. Schulte Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvent Eur. Biophys. J. 26 1997 327 335
    • (1997) Eur. Biophys. J. , vol.26 , pp. 327-335
    • Demmel, F.1    Doster, W.2    Petry, W.3    Schulte, A.4
  • 86
    • 0344651045 scopus 로고    scopus 로고
    • Protein-solvent interactions and biological functions. Models from statistical physics
    • H. Frauenfelder G. Hummer R. Garcia AIP American Institute of Physics Melville, NY
    • G. Careri Protein-solvent interactions and biological functions. Models from statistical physics H. Frauenfelder G. Hummer R. Garcia Biological Physics 1999 AIP American Institute of Physics Melville, NY 8 13
    • (1999) Biological Physics , pp. 8-13
    • Careri, G.1
  • 87
    • 0022762471 scopus 로고
    • Thermal properties of water in myoglobin crystals and solutions at subzero temperatures
    • W. Doster, A. Bacheitner, R. Dunau, M. Hiebl, and E. Luscher Thermal properties of water in myoglobin crystals and solutions at subzero temperatures Biophys. J. 50 1986 213 219
    • (1986) Biophys. J. , vol.50 , pp. 213-219
    • Doster, W.1    Bacheitner, A.2    Dunau, R.3    Hiebl, M.4    Luscher, E.5
  • 88
    • 0000385590 scopus 로고
    • The protein-glass analogy: New insight from homopeptide comparisons
    • J.L. Green, J. Fan, and C.A. Angell The protein-glass analogy: new insight from homopeptide comparisons J. Phys. Chem. 98 1994 13780 13790
    • (1994) J. Phys. Chem. , vol.98 , pp. 13780-13790
    • Green, J.L.1    Fan, J.2    Angell, C.A.3
  • 89
    • 0024952939 scopus 로고
    • Protein and protein-bound water dynamics studied by rayleigh scattering of Mössbauer radiation (RSMR)
    • V.I. Goldanskii, and Y.F. Krupyanskii Protein and protein-bound water dynamics studied by rayleigh scattering of Mössbauer radiation (RSMR) Q. Rev. Biophys. 22 1989 39 92
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 39-92
    • Goldanskii, V.I.1    Krupyanskii, Y.F.2
  • 90
    • 0030853055 scopus 로고    scopus 로고
    • The lubricant of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure
    • L.D. Barron, L. Hecht, and G. Wilson The lubricant of life: a proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure Biochemistry 36 1997 13143 13147
    • (1997) Biochemistry , vol.36 , pp. 13143-13147
    • Barron, L.D.1    Hecht, L.2    Wilson, G.3
  • 91
    • 5144223810 scopus 로고    scopus 로고
    • Bulk solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuation in glasses, control protein motions and functions
    • P.W. Fenimore, H. Frauenfelder, B.H. McMahon, and R.D. Young Bulk solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuation in glasses, control protein motions and functions Proc. Natl. Acad. Sci. U. S. A. 101 2004 14408 14413
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14408-14413
    • Fenimore, P.W.1    Frauenfelder, H.2    McMahon, B.H.3    Young, R.D.4
  • 92
    • 16344396586 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sucrose coated and trehalose coated carboxy-myoglobin
    • G. Cottone, S. Giuffrida, G. Ciccotti, and L. Cordone Molecular dynamics simulation of sucrose coated and trehalose coated carboxy-myoglobin Proteins 59 2005 291 302
    • (2005) Proteins , vol.59 , pp. 291-302
    • Cottone, G.1    Giuffrida, S.2    Ciccotti, G.3    Cordone, L.4
  • 93
    • 0020712534 scopus 로고
    • Preservation of structural and functional activity in lyophilized sarcoplasmic reticulum
    • J.H. Crowe, L.M. Crowe, and S.A. Jackson Preservation of structural and functional activity in lyophilized sarcoplasmic reticulum Arch. Biochem. Biophys. 220 1983 615 617
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 615-617
    • Crowe, J.H.1    Crowe, L.M.2    Jackson, S.A.3
  • 95
    • 0442311060 scopus 로고    scopus 로고
    • Probing solvation-shell hydrogen binding in glassy and sol-gel matrices through vibronic sideband luminescence spectroscopy
    • M.S. Navati, A. Ray, J. Shamir, and J.M. Friedman Probing solvation-shell hydrogen binding in glassy and sol-gel matrices through vibronic sideband luminescence spectroscopy J. Phys. Chem., B 108 2004 1321 1327
    • (2004) J. Phys. Chem., B , vol.108 , pp. 1321-1327
    • Navati, M.S.1    Ray, A.2    Shamir, J.3    Friedman, J.M.4
  • 99
    • 0344730727 scopus 로고
    • Protein fluctuations, distributed coupling, and the binding of ligands to heme proteins
    • V. Srajer, L. Reinisch, and P.M. Champion Protein fluctuations, distributed coupling, and the binding of ligands to heme proteins J. Am. Chem. Soc. 110 1988 6656 6670
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 6656-6670
    • Srajer, V.1    Reinisch, L.2    Champion, P.M.3
  • 100
    • 0025845767 scopus 로고
    • Ligand binding to heme proteins: Connection between dynamics and function
    • P.J. Steinbach Ligand binding to heme proteins: connection between dynamics and function Biochemistry 30 1991 3988 4001
    • (1991) Biochemistry , vol.30 , pp. 3988-4001
    • Steinbach, P.J.1
  • 102
    • 0027319374 scopus 로고
    • Structural relaxation and nonexponential kinetics of CO binding to horse myoglobin. Multiple flash photolysis experiments
    • F. Post, W. Doster, G. Karvounis, and M. Settles Structural relaxation and nonexponential kinetics of CO binding to horse myoglobin. Multiple flash photolysis experiments Biophys. J. 64 1993 1833 1842
    • (1993) Biophys. J. , vol.64 , pp. 1833-1842
    • Post, F.1    Doster, W.2    Karvounis, G.3    Settles, M.4
  • 105
    • 0032534909 scopus 로고    scopus 로고
    • Spectroscopic evidence for nanosecond protein relaxation after photodissociation of myoglobin-CO
    • R.M. Esquerra, R.A. Goldbeck, D.B. Kim-Shapiro, and D.S. Kliger Spectroscopic evidence for nanosecond protein relaxation after photodissociation of myoglobin-CO Biochemistry 37 1998 17527 17536
    • (1998) Biochemistry , vol.37 , pp. 17527-17536
    • Esquerra, R.M.1    Goldbeck, R.A.2    Kim-Shapiro, D.B.3    Kliger, D.S.4
  • 107
    • 0346057931 scopus 로고    scopus 로고
    • Competition with xenon elicits ligand migration and escape pathways in myoglobin
    • C. Tetreau, Y. Blouquit, E. Novikov, E. Quiniou, and D. Lavalette Competition with xenon elicits ligand migration and escape pathways in myoglobin Biophys. J. 86 2004 435 447
    • (2004) Biophys. J. , vol.86 , pp. 435-447
    • Tetreau, C.1    Blouquit, Y.2    Novikov, E.3    Quiniou, E.4    Lavalette, D.5
  • 108
    • 0028077565 scopus 로고
    • Crystal structure of photolysed carbonmonoxy-myoglobin
    • I. Schlichting, J. Berendzen, G.N. Phillips, and R.M. Sweet Crystal structure of photolysed carbonmonoxy-myoglobin Nature 371 1994 808 812
    • (1994) Nature , vol.371 , pp. 808-812
    • Schlichting, I.1    Berendzen, J.2    Phillips, G.N.3    Sweet, R.M.4
  • 111
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • A. Ostermann, R. Washipky, F. Parak, and G.U. Nienhaus Ligand binding and conformational motions in myoglobin Nature 404 2000 205 208
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Washipky, R.2    Parak, F.3    Nienhaus, G.U.4
  • 112
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • J.S. Olson, and G.N. Phillips Kinetic pathways and barriers for ligand binding to myoglobin J. Biol. Chem. 271 1996 17593 17596
    • (1996) J. Biol. Chem. , vol.271 , pp. 17593-17596
    • Olson, J.S.1    Phillips, G.N.2
  • 113
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved laue X-ray diffraction
    • V. Srajer, Z. Ren, T.Y. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff, and K. Moffat Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved laue X-ray diffraction Biochemistry 40 2001 13802 13815
    • (2001) Biochemistry , vol.40 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 115
    • 2942655520 scopus 로고    scopus 로고
    • Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin
    • C. Bossa, M. Anselmi, D. Roccatano, A. Amadei, B. Vallone, M. Brunori, and A.D. Nola Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin Biophys. J. 86 2004 3855 3862
    • (2004) Biophys. J. , vol.86 , pp. 3855-3862
    • Bossa, C.1    Anselmi, M.2    Roccatano, D.3    Amadei, A.4    Vallone, B.5    Brunori, M.6    Nola, A.D.7
  • 116
    • 0027502033 scopus 로고
    • CO recombination to human myoglobin mutants in glycerol-water solutions
    • S. Balasubramanian, D.G. Lambright, M.C. Marden, and S.G. Boxer CO recombination to human myoglobin mutants in glycerol-water solutions Biochemistry 32 1993 2202 2212
    • (1993) Biochemistry , vol.32 , pp. 2202-2212
    • Balasubramanian, S.1    Lambright, D.G.2    Marden, M.C.3    Boxer, S.G.4
  • 117
    • 3042690149 scopus 로고    scopus 로고
    • Protein relaxation in the photodissociation of myoglobin-CO complex
    • L. Angeloni, and A. Feis Protein relaxation in the photodissociation of myoglobin-CO complex Photochem. Photobiol. Sci. 2 2003 730 740
    • (2003) Photochem. Photobiol. Sci. , vol.2 , pp. 730-740
    • Angeloni, L.1    Feis, A.2
  • 118
    • 4444253708 scopus 로고    scopus 로고
    • Coupling of protein relaxation to ligand binding and migration in myoglobin
    • N. Agmon Coupling of protein relaxation to ligand binding and migration in myoglobin Biophys. J. 87 2004 1537 1543
    • (2004) Biophys. J. , vol.87 , pp. 1537-1543
    • Agmon, N.1
  • 119
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobin
    • M. Brunori, and Q.H. Gibson Cavities and packing defects in the structural dynamics of myoglobin EMBO Rep. 2 2001 674 679
    • (2001) EMBO Rep. , vol.2 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 120
    • 0030768765 scopus 로고    scopus 로고
    • Ligand migration in sperm whale myoglobin
    • E.E. Scott, and Q.H. Gibson Ligand migration in sperm whale myoglobin Biochemistry 36 1997 11909 11917
    • (1997) Biochemistry , vol.36 , pp. 11909-11917
    • Scott, E.E.1    Gibson, Q.H.2
  • 121
    • 0035895937 scopus 로고    scopus 로고
    • Mapping the pathways for O2 entry into and exit from myoglobin
    • E.E. Scott, Q.H. Gibson, and J.S. Olson Mapping the pathways for O2 entry into and exit from myoglobin J. Biol. Chem. 276 2001 5177 5188
    • (2001) J. Biol. Chem. , vol.276 , pp. 5177-5188
    • Scott, E.E.1    Gibson, Q.H.2    Olson, J.S.3
  • 123
    • 0037461332 scopus 로고    scopus 로고
    • Quaternary structure dependance of kinetic hole burning and conformational substates interconversion in hemoglobin
    • M. Levantino, A. Cupane, and L. Zimanyi Quaternary structure dependance of kinetic hole burning and conformational substates interconversion in hemoglobin Biochemistry 42 2003 4499 4505
    • (2003) Biochemistry , vol.42 , pp. 4499-4505
    • Levantino, M.1    Cupane, A.2    Zimanyi, L.3
  • 124
    • 0021818674 scopus 로고
    • Structure, dynamics and reactivity in hemoglobin
    • J.M. Friedman Structure, dynamics and reactivity in hemoglobin Science 228 1985 1273 1280
    • (1985) Science , vol.228 , pp. 1273-1280
    • Friedman, J.M.1
  • 127
    • 0037414277 scopus 로고    scopus 로고
    • Oxygen equilibrium properties of myoglobin locked in the liganded and unliganded conformations
    • N. Shibayama, and S. Saigo Oxygen equilibrium properties of myoglobin locked in the liganded and unliganded conformations J. Am. Chem. Soc. 125 2003 3780 3783
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3780-3783
    • Shibayama, N.1    Saigo, S.2
  • 128
    • 0037067708 scopus 로고    scopus 로고
    • Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin
    • U. Samuni, D. Dantsker, I. Khan, A.J. Friedman, E. Peterson, and J.M. Friedman Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin J. Biol. Chem. 277 2002 25783 25790
    • (2002) J. Biol. Chem. , vol.277 , pp. 25783-25790
    • Samuni, U.1    Dantsker, D.2    Khan, I.3    Friedman, A.J.4    Peterson, E.5    Friedman, J.M.6
  • 129
    • 0036863052 scopus 로고    scopus 로고
    • Inferring lifetime distributions from kinetics by maximizing entropy using a bootstrapped model
    • P.J. Steinbach Inferring lifetime distributions from kinetics by maximizing entropy using a bootstrapped model J. Chem. Inf. Comput. Sci. 42 2002 1476 1478
    • (2002) J. Chem. Inf. Comput. Sci. , vol.42 , pp. 1476-1478
    • Steinbach, P.J.1
  • 130
    • 0036212631 scopus 로고    scopus 로고
    • Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least- squares method: Application to protein folding
    • P.J. Steinbach, R. Ionescu, and C.R. Matthews Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: application to protein folding Biophys. J. 82 2002 2244 2255
    • (2002) Biophys. J. , vol.82 , pp. 2244-2255
    • Steinbach, P.J.1    Ionescu, R.2    Matthews, C.R.3
  • 133
    • 0034734278 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin
    • M. Brunori Structural dynamics of myoglobin Biophys. Chem. 86 2000 221 230
    • (2000) Biophys. Chem. , vol.86 , pp. 221-230
    • Brunori, M.1
  • 134
    • 0000058886 scopus 로고
    • Structure and function of bacterial photosynthetic reaction centres
    • G. Feher, J.P. Allen, M.Y. Okamura, and D.C. Rees Structure and function of bacterial photosynthetic reaction centres Nature 33 1989 111 116
    • (1989) Nature , vol.33 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 135
    • 0000603608 scopus 로고
    • Electron and proton transfer in the acceptor quinone complex of reaction centers of phototrophic bacteria
    • J. Deisenhofer J.R. Norris Academic Press San Diego
    • V.P. Shinkarev, and C.A. Wraight Electron and proton transfer in the acceptor quinone complex of reaction centers of phototrophic bacteria J. Deisenhofer J.R. Norris The Photosynthetic Reaction Center vol. 1 1993 Academic Press San Diego 193 255
    • (1993) The Photosynthetic Reaction Center , vol.1 , pp. 193-255
    • Shinkarev, V.P.1    Wraight, C.A.2
  • 136
    • 0000230806 scopus 로고
    • The reaction center protein from purple bacteria: Structure and function
    • M.R. Gunner The reaction center protein from purple bacteria: structure and function Curr. Top. Bioenerg. 16 1991 319 367
    • (1991) Curr. Top. Bioenerg. , vol.16 , pp. 319-367
    • Gunner, M.R.1
  • 137
    • 84985164554 scopus 로고
    • Oxidation-reduction physical chemistry of the acceptor quinone complex in bacterial photosynthetic reaction centers: Evidence for a new model of herbicide activity
    • C.A. Wraight Oxidation-reduction physical chemistry of the acceptor quinone complex in bacterial photosynthetic reaction centers: evidence for a new model of herbicide activity Isr. J. Chem. 21 1981 348 354
    • (1981) Isr. J. Chem. , vol.21 , pp. 348-354
    • Wraight, C.A.1
  • 139
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • A.R. Crofts, and C.A. Wraight The electrochemical domain of photosynthesis Biochim. Biophys. Acta 726 1983 149 185
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 141
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • R.A. Marcus, and N. Sutin Electron transfer in chemistry and biology Biochim. Biophys. Acta 811 1985 265 322
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 142
    • 21744452904 scopus 로고
    • Coupling of protein motion to electron transfer in a photosynthetic reaction center: Investigating the low temperature behavior in the framework of the spin-boson model
    • D. Xu, and K. Schulten Coupling of protein motion to electron transfer in a photosynthetic reaction center: investigating the low temperature behavior in the framework of the spin-boson model Chem. Phys. 182 1994 91 117
    • (1994) Chem. Phys. , vol.182 , pp. 91-117
    • Xu, D.1    Schulten, K.2
  • 143
    • 0021674417 scopus 로고
    • Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes
    • D. Kleinfeld, M.Y. Okamura, and G. Feher Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes Biochemistry 23 1984 5780 5786
    • (1984) Biochemistry , vol.23 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 144
    • 0019878636 scopus 로고
    • Enthalpy and volume changes accompanying electron transfer from P870 to quinones in Rhodopseudomonas sphaeroides reaction centers
    • H. Arata, and W.W. Parson Enthalpy and volume changes accompanying electron transfer from P870 to quinones in Rhodopseudomonas sphaeroides reaction centers Biochim. Biophys. Acta, Bioenerg. 636 1981 70 81
    • (1981) Biochim. Biophys. Acta, Bioenerg. , vol.636 , pp. 70-81
    • Arata, H.1    Parson, W.W.2
  • 145
    • 0028301764 scopus 로고
    • Photochemical energy storage and volume changes in the microsecond time range in bacterial photosynthesis-A laser induced optoacoustic study
    • S. Malkin, M.S. Churio, S. Shochat, and S.E. Braslavsky Photochemical energy storage and volume changes in the microsecond time range in bacterial photosynthesis-A laser induced optoacoustic study J. Photochem. Photobiol., B Biol. 23 1994 79 85
    • (1994) J. Photochem. Photobiol., B Biol. , vol.23 , pp. 79-85
    • Malkin, S.1    Churio, M.S.2    Shochat, S.3    Braslavsky, S.E.4
  • 146
    • 0028831367 scopus 로고
    • The volume contraction of photoexcitation of the reaction center from R. sphaeroides R-26: An internal probe of dielectrics
    • D.C. Mauzerall, M.R. Gunner, and J.W. Zhang The volume contraction of photoexcitation of the reaction center from R. sphaeroides R-26: an internal probe of dielectrics Biophys. J. 68 1995 275 280
    • (1995) Biophys. J. , vol.68 , pp. 275-280
    • Mauzerall, D.C.1    Gunner, M.R.2    Zhang, J.W.3
  • 147
    • 0029016874 scopus 로고
    • Trypsin treatment of reaction centers from Rhodobacter sphaeroides in the dark and under illumination: Protein structural changes follow charge separation
    • P. Brzezinski, and L.E. Andreasson Trypsin treatment of reaction centers from Rhodobacter sphaeroides in the dark and under illumination: protein structural changes follow charge separation Biochemistry 34 1995 7498 7506
    • (1995) Biochemistry , vol.34 , pp. 7498-7506
    • Brzezinski, P.1    Andreasson, L.E.2
  • 148
    • 0038479088 scopus 로고    scopus 로고
    • Conformational-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides
    • L. Kalman, and P. Maroti Conformational-activated protonation in reaction centers of the photosynthetic bacterium Rhodobacter sphaeroides Biochemistry 36 1997 15269 15276
    • (1997) Biochemistry , vol.36 , pp. 15269-15276
    • Kalman, L.1    Maroti, P.2
  • 149
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implication for mechanism of electron-proton transfer
    • M.H.B. Stowell, T.M. McPhillips, D.C. Rees, S.M. Soltis, E. Abresch, and G. Feher Light-induced structural changes in photosynthetic reaction center: implication for mechanism of electron-proton transfer Science 276 1997 812 816
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 151
    • 0344193626 scopus 로고    scopus 로고
    • Electron transfer and protein dynamics in the photosynthetic reaction center
    • B.H. McMahon, J.D. Müller, C.A. Wraight, and G.U. Nienhaus Electron transfer and protein dynamics in the photosynthetic reaction center Biophys. J. 74 1998 2567 2587
    • (1998) Biophys. J. , vol.74 , pp. 2567-2587
    • McMahon, B.H.1    Müller, J.D.2    Wraight, C.A.3    Nienhaus, G.U.4
  • 152
    • 0032578541 scopus 로고    scopus 로고
    • - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay
    • - in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay Proc. Natl. Acad. Sci. U. S. A. 95 1998 11679 11684
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11679-11684
    • Graige, M.S.1    Feher, G.2    Okamura, M.Y.3
  • 154
    • 0041821411 scopus 로고    scopus 로고
    • Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix
    • J.M. Kriegl, F.K. Forster, and G.U. Nienhaus Charge recombination and protein dynamics in bacterial photosynthetic reaction centers entrapped in a sol-gel matrix Biophys. J. 85 2003 1851 1870
    • (2003) Biophys. J. , vol.85 , pp. 1851-1870
    • Kriegl, J.M.1    Forster, F.K.2    Nienhaus, G.U.3
  • 155
    • 0345827604 scopus 로고    scopus 로고
    • Structural, dynamic, and energetic aspects of long-range electron transfer in photosynthetic reaction centers
    • J.M. Kriegl, and G.U. Nienhaus Structural, dynamic, and energetic aspects of long-range electron transfer in photosynthetic reaction centers Proc. Natl. Acad. Sci. U. S. A. 101 2004 123 128
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 123-128
    • Kriegl, J.M.1    Nienhaus, G.U.2
  • 156
    • 0002735129 scopus 로고
    • - reaction in isolated reaction centers from the photosynthetic bacterium Rhodobacter sphaeroides
    • - reaction in isolated reaction centers from the photosynthetic bacterium Rhodobacter sphaeroides Biochim. Biophys. Acta, Bioenerg. 764 1984 46 54
    • (1984) Biochim. Biophys. Acta, Bioenerg. , vol.764 , pp. 46-54
    • Mancino, L.1    Dean, D.2    Blankenship, R.3
  • 157
    • 0029769668 scopus 로고    scopus 로고
    • Time-resolved electrochromism center associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction
    • D.M. Tiede, J. Vazquez, J. Cordova, and P.A. Marone Time-resolved electrochromism center associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction Biochemistry 35 1996 10763 10775
    • (1996) Biochemistry , vol.35 , pp. 10763-10775
    • Tiede, D.M.1    Vazquez, J.2    Cordova, J.3    Marone, P.A.4
  • 158
    • 0032478280 scopus 로고    scopus 로고
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers Biochemistry 37 1998 2818 2829
    • (1998) Biochemistry , vol.37 , pp. 2818-2829
    • Li, J.1    Gilroy, D.2    Tiede, D.M.3    Gunner, M.R.4
  • 161
    • 0035852970 scopus 로고    scopus 로고
    • Trapping conformational intermediate states in the reaction center protein from photosynthetic bacteria
    • Q. Xu, and M.R. Gunner Trapping conformational intermediate states in the reaction center protein from photosynthetic bacteria Biochemistry 40 2001 3232 3241
    • (2001) Biochemistry , vol.40 , pp. 3232-3241
    • Xu, Q.1    Gunner, M.R.2
  • 162
    • 0035836485 scopus 로고    scopus 로고
    • X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: Structural changes induced by point mutations at position L209 modulate electron and proton transfer
    • A. Kuglstatter, U. Emler, H. Michel, L. Baciou, and G. Fritzsch X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: structural changes induced by point mutations at position L209 modulate electron and proton transfer Biochemistry 40 2001 4253 4260
    • (2001) Biochemistry , vol.40 , pp. 4253-4260
    • Kuglstatter, A.1    Emler, U.2    Michel, H.3    Baciou, L.4    Fritzsch, G.5
  • 163
    • 0037195263 scopus 로고    scopus 로고
    • B binding site at the proximal position in wild-type reaction centers and in the Pro-L209→Tyr mutant from Rhodobacter sphaeroides
    • B binding site at the proximal position in wild-type reaction centers and in the Pro-L209→Tyr mutant from Rhodobacter sphaeroides Biochemistry 41 2002 12921 12927
    • (2002) Biochemistry , vol.41 , pp. 12921-12927
    • Breton, J.1    Boullais, C.2    Mioskowsky, C.3    Sebban, P.4    Baciou, L.5    Nabedryk, E.6
  • 164
    • 1642361308 scopus 로고    scopus 로고
    • B in bacterial photosynthetic reaction centers
    • B in bacterial photosynthetic reaction centers Biochemistry 43 2004 3318 3326
    • (2004) Biochemistry , vol.43 , pp. 3318-3326
    • Breton, J.1
  • 165
    • 0037176849 scopus 로고    scopus 로고
    • B electron transfer reaction in bacterial photosynthetic reaction centers: PH dependence of the conformational gating step
    • B electron transfer reaction in bacterial photosynthetic reaction centers: pH dependence of the conformational gating step Biochemistry 41 2002 2694 2701
    • (2002) Biochemistry , vol.41 , pp. 2694-2701
    • Xu, Q.1    Gunner, M.R.2
  • 166
    • 0033614791 scopus 로고    scopus 로고
    • B in bacterial photosynthetic reaction centers
    • B in bacterial photosynthetic reaction centers Biochemistry 38 1999 8253 8270
    • (1999) Biochemistry , vol.38 , pp. 8253-8270
    • Alexov, E.G.1    Gunner, M.R.2
  • 167
    • 0001178664 scopus 로고    scopus 로고
    • Amino acid protonation states determine binding sites of the secondary ubiquinone and its anion in the Rhodobacter sphaeroides photosynthetic reaction center
    • A.K. Grafton, and R.A. Wheeler Amino acid protonation states determine binding sites of the secondary ubiquinone and its anion in the Rhodobacter sphaeroides photosynthetic reaction center J. Phys. Chem., B 103 1999 5380 5387
    • (1999) J. Phys. Chem., B , vol.103 , pp. 5380-5387
    • Grafton, A.K.1    Wheeler, R.A.2
  • 168
    • 0034730115 scopus 로고    scopus 로고
    • Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes
    • B. Rabenstein, G. Matthias Ullmann, and E.-W. Knapp Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes Biochemistry 39 2000 10487 10496
    • (2000) Biochemistry , vol.39 , pp. 10487-10496
    • Rabenstein, B.1    Matthias Ullmann, G.2    Knapp, E.-W.3
  • 169
    • 0037149804 scopus 로고    scopus 로고
    • Protein conformational gate controlling binding site preference and migration for ubiquinone-B in the photosynthetic reaction center of Rhodobacter sphaeroides
    • S.E. Walden, and R.A. Wheeler Protein conformational gate controlling binding site preference and migration for ubiquinone-B in the photosynthetic reaction center of Rhodobacter sphaeroides J. Phys. Chem., B 106 2002 3001 3006
    • (2002) J. Phys. Chem., B , vol.106 , pp. 3001-3006
    • Walden, S.E.1    Wheeler, R.A.2
  • 170
    • 2442536910 scopus 로고    scopus 로고
    • Potential energy landscape for conformationally gated secondary ubiquinone binding in the photosynthetic reaction center of Rhodobacter sphaeroides
    • A. Rahaman, and R.A. Wheeler Potential energy landscape for conformationally gated secondary ubiquinone binding in the photosynthetic reaction center of Rhodobacter sphaeroides Chem. Phys. Chem. 5 2004 249 252
    • (2004) Chem. Phys. Chem. , vol.5 , pp. 249-252
    • Rahaman, A.1    Wheeler, R.A.2
  • 171
    • 0035114672 scopus 로고    scopus 로고
    • Photosynthetic electron transfer controlled by protein relaxation: Analysis by Langevin stochastic approach
    • D.A. Cherepanov, L.I. Krishtalik, and A.Y. Mulkidjanian Photosynthetic electron transfer controlled by protein relaxation: analysis by Langevin stochastic approach Biophys. J. 80 2001 1033 1049
    • (2001) Biophys. J. , vol.80 , pp. 1033-1049
    • Cherepanov, D.A.1    Krishtalik, L.I.2    Mulkidjanian, A.Y.3
  • 172
    • 0037031293 scopus 로고    scopus 로고
    • B electron transfer in bacterial photosynthetic reaction centers: Effect of substrate position and tail length on the conformational gating step
    • B electron transfer in bacterial photosynthetic reaction centers: effect of substrate position and tail length on the conformational gating step Biochemistry 41 2002 10021 10025
    • (2002) Biochemistry , vol.41 , pp. 10021-10025
    • Xu, Q.1    Baciou, L.2    Sebban, P.3    Gunner, M.R.4
  • 173
    • 0025219483 scopus 로고
    • Thermal behavior of the 760 nm band in photodissociated sperm whale myoglobin at cryogenic temperatures: Dependence on external medium
    • L. Cordone, A. Cupane, M. Leone, and E. Vitrano Thermal behavior of the 760 nm band in photodissociated sperm whale myoglobin at cryogenic temperatures: dependence on external medium Biopolymers 29 1990 639 643
    • (1990) Biopolymers , vol.29 , pp. 639-643
    • Cordone, L.1    Cupane, A.2    Leone, M.3    Vitrano, E.4
  • 174
    • 0035073849 scopus 로고    scopus 로고
    • Trehalose effect on low temperature protein dynamics: Fluctuation and relaxation phenomena
    • J. Schlichter, J. Friedrich, L. Herenyi, and J. Fidy Trehalose effect on low temperature protein dynamics: fluctuation and relaxation phenomena Biophys. J. 80 2001 2011 2017
    • (2001) Biophys. J. , vol.80 , pp. 2011-2017
    • Schlichter, J.1    Friedrich, J.2    Herenyi, L.3    Fidy, J.4
  • 176
    • 0031949427 scopus 로고    scopus 로고
    • Physics and biophysics of solvent induced forces: Hydrophobic interactions and context-dependent hydration
    • P.L. San Biagio, D. Bulone, V. Martorana, M.B. Palma-Vittorelli, and M.U. Palma Physics and biophysics of solvent induced forces: hydrophobic interactions and context-dependent hydration Eur. Biophys. J. 27 1998 183 196
    • (1998) Eur. Biophys. J. , vol.27 , pp. 183-196
    • San Biagio, P.L.1    Bulone, D.2    Martorana, V.3    Palma-Vittorelli, M.B.4    Palma, M.U.5
  • 178
    • 0032147029 scopus 로고    scopus 로고
    • Interaction of explicit solvent with hydrophobic/philic/charged residues of a protein: Residue character vs. conformational context
    • V. Martorana, G. Corongiu, and M.U. Palma Interaction of explicit solvent with hydrophobic/philic/charged residues of a protein: residue character vs. conformational context Proteins 32 1998 129 135
    • (1998) Proteins , vol.32 , pp. 129-135
    • Martorana, V.1    Corongiu, G.2    Palma, M.U.3
  • 180
    • 0032757309 scopus 로고    scopus 로고
    • Solvent-induced free energy landscape and solute-solvent dynamic coupling in a multielement solute
    • P.L. San Biagio, V. Martorana, D. Bulone, M.B. Palma-Vittorelli, and M.U. Palma Solvent-induced free energy landscape and solute-solvent dynamic coupling in a multielement solute Biophys. J. 77 1999 2470 2478
    • (1999) Biophys. J. , vol.77 , pp. 2470-2478
    • San Biagio, P.L.1    Martorana, V.2    Bulone, D.3    Palma-Vittorelli, M.B.4    Palma, M.U.5
  • 181
    • 0030607925 scopus 로고    scopus 로고
    • Correlated solvent-induced forces on a protein at single residue resolution: Relation to conformation, stability, dynamics and function
    • V. Martorana, G. Corongiu, and M.U. Palma Correlated solvent-induced forces on a protein at single residue resolution: relation to conformation, stability, dynamics and function Chem. Phys. Lett. 254 1996 292 301
    • (1996) Chem. Phys. Lett. , vol.254 , pp. 292-301
    • Martorana, V.1    Corongiu, G.2    Palma, M.U.3
  • 182
  • 183
    • 51249181147 scopus 로고
    • Effect of monohydric alcohols on structural properties of macromolecular solutions
    • R. Giordano, F. Wanderlingh, L. Cordone, and A. Cupane Effect of monohydric alcohols on structural properties of macromolecular solutions Il Nuovo Cim. 2D 1983 47 54
    • (1983) Il Nuovo Cim. , vol.2 , pp. 47-54
    • Giordano, R.1    Wanderlingh, F.2    Cordone, L.3    Cupane, A.4
  • 184
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins
    • P.H. von Hippel, and K.Y. Wong On the conformational stability of globular proteins J. Biol. Chem. 940 1965 3909 3923
    • (1965) J. Biol. Chem. , vol.940 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 185
    • 0018324767 scopus 로고
    • Effects of some monohydric alcohols on the functional stability of bovine liver B-galactosidase
    • L. Cordone, V. Izzo, G. Sgroi, and S.L. Fornili Effects of some monohydric alcohols on the functional stability of bovine liver B-galactosidase Biopolymers 18 1979 1965 1974
    • (1979) Biopolymers , vol.18 , pp. 1965-1974
    • Cordone, L.1    Izzo, V.2    Sgroi, G.3    Fornili, S.L.4
  • 186
    • 0019484348 scopus 로고
    • Effects of some organic cosolvents on the reaction of hemoglobin with oxygen
    • L. Cordone, A. Cupane, P.L. San Biagio, and E. Vitrano Effects of some organic cosolvents on the reaction of hemoglobin with oxygen Biopolymers 20 1981 39 51
    • (1981) Biopolymers , vol.20 , pp. 39-51
    • Cordone, L.1    Cupane, A.2    San Biagio, P.L.3    Vitrano, E.4
  • 187
    • 0019400116 scopus 로고
    • Temperature dependence of the effects of some monohydric alcohols on the oxygen affinity of hemoglobin: Determination and analysis of thermodinamic parameters
    • L. Cordone, A. Cupane, P.L. San Biagio, and E. Vitrano Temperature dependence of the effects of some monohydric alcohols on the oxygen affinity of hemoglobin: determination and analysis of thermodinamic parameters Biopolymers 20 1981 53 63
    • (1981) Biopolymers , vol.20 , pp. 53-63
    • Cordone, L.1    Cupane, A.2    San Biagio, P.L.3    Vitrano, E.4
  • 188
    • 0023053402 scopus 로고
    • Effects of organic cosolvents on the oxygen equilibrium of human hemoglobin
    • L. Cordone, A. Cupane, and E. Vitrano Effects of organic cosolvents on the oxygen equilibrium of human hemoglobin J. Mol. Biol. 189 1986 343 351
    • (1986) J. Mol. Biol. , vol.189 , pp. 343-351
    • Cordone, L.1    Cupane, A.2    Vitrano, E.3
  • 189
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • S.N. Timasheff Protein hydration, thermodynamic binding, and preferential hydration Biochemistry 41 2002 13473 13482
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1


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