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Volumn 93, Issue 1, 2007, Pages 284-293

GFP-mut2 proteins in trehalose-water matrixes: Spatially heterogeneous protein-water-sugar structures

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; GLASS; GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN; SUGAR; TREHALOSE; WATER;

EID: 34447254697     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.090621     Document Type: Article
Times cited : (10)

References (58)
  • 1
    • 0036182386 scopus 로고    scopus 로고
    • Lesson from nature: A role of sugars in anhydrobiosis
    • Crowe, L. M. 2002. Lesson from nature: a role of sugars in anhydrobiosis. Comp. Biochem. Physiol. A. 132:505-513.
    • (2002) Comp. Biochem. Physiol. A , vol.132 , pp. 505-513
    • Crowe, L.M.1
  • 3
    • 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. (Tokyo). 117:774-779.
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 774-779
    • Uritani, M.1    Takai, M.2    Yoshinaga, K.3
  • 4
    • 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
  • 5
    • 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
  • 6
    • 0020712534 scopus 로고
    • Preservation of structural and functional activity in lyophilized sarcoplasmic reticulum
    • Crowe, J. H., L. M. Crowe, and S. A. Jackson. 1983. Preservation of structural and functional activity in lyophilized sarcoplasmic reticulum. Arch. Biochem. Biophys. 220:615-617.
    • (1983) Arch. Biochem. Biophys , vol.220 , pp. 615-617
    • Crowe, J.H.1    Crowe, L.M.2    Jackson, S.A.3
  • 7
    • 85030500484 scopus 로고    scopus 로고
    • Crowe, L. M., and J. H. Crowe. 1995. Freeze-dried liposomes. In Liposomes, New Systems and New Trends in Their Applications. F. Puisieux, P. Covreur, L. Delattre, and J. P. Devissaguet, editors. Editions de Santè, Paris. 237-272.
    • Crowe, L. M., and J. H. Crowe. 1995. Freeze-dried liposomes. In Liposomes, New Systems and New Trends in Their Applications. F. Puisieux, P. Covreur, L. Delattre, and J. P. Devissaguet, editors. Editions de Santè, Paris. 237-272.
  • 8
    • 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
  • 10
    • 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
  • 11
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    • Cordone, L., M. Ferrand, E. Vitrano, and G. Zaccai. 1999. Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biophys. J. 76:1043-1047.
    • (1999) Biophys. J , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 12
    • 0035250097 scopus 로고    scopus 로고
    • Effects of solvent viscosity on protein dynamics: Infrared vibrational echo experiments and theory
    • Rector, D., J. Jiang, M. A. Berg, and M. D. Fayer. 2001. Effects of solvent viscosity on protein dynamics: infrared vibrational echo experiments and theory. J. Phys. Chem. B. 105:1081-1092.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 1081-1092
    • Rector, D.1    Jiang, J.2    Berg, M.A.3    Fayer, M.D.4
  • 13
    • 0035073849 scopus 로고    scopus 로고
    • Trehalose effect on low temperature protein dynamics: Fluctuation and relaxation phenomena
    • Schlichter, J., J. Friedrich, L. Herenyi, and J. Fidy. 2001. Trehalose effect on low temperature protein dynamics: fluctuation and relaxation phenomena. Biophys. J. 80:2011-2017.
    • (2001) Biophys. J , vol.80 , pp. 2011-2017
    • Schlichter, J.1    Friedrich, J.2    Herenyi, L.3    Fidy, J.4
  • 14
    • 0036733803 scopus 로고    scopus 로고
    • Solvent effect on conformational dynamics of proteins: Cytochrome c in a dried trehalose film
    • Ponkratov, V. V., J. Friedrich, and J. M. Vanderkooi. 2002. Solvent effect on conformational dynamics of proteins: cytochrome c in a dried trehalose film. J. Chem. Phys. 117:4594-4601.
    • (2002) J. Chem. Phys , vol.117 , pp. 4594-4601
    • Ponkratov, V.V.1    Friedrich, J.2    Vanderkooi, J.M.3
  • 15
    • 0036156512 scopus 로고    scopus 로고
    • Electron transfer in photosynthetic reaction center embedded in trehalose glasses: Trapping of conformational substates at room temperature
    • Palazzo, G., A. Mallardi, A. Hochkoeppler, L. Cordone, and G. Venturoli. 2002. Electron transfer in photosynthetic reaction center embedded in trehalose glasses: trapping of conformational substates at room temperature. Biophys. J. 82:558-568.
    • (2002) Biophys. J , vol.82 , pp. 558-568
    • Palazzo, G.1    Mallardi, A.2    Hochkoeppler, A.3    Cordone, L.4    Venturoli, G.5
  • 17
    • 3543046791 scopus 로고    scopus 로고
    • Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrixes
    • Francia, F., G. Palazzo, A. Mallardi, L. Cordone, and G. Venturoli. 2004. Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrixes. Biochim. Biophys. Acta. 1658:50-57.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 50-57
    • Francia, F.1    Palazzo, G.2    Mallardi, A.3    Cordone, L.4    Venturoli, G.5
  • 18
    • 0035144443 scopus 로고    scopus 로고
    • Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix
    • Cottone, G., L. Cordone, and G. Ciccotti. 2001. Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix. Biophys. J. 80:931-938.
    • (2001) Biophys. J , vol.80 , pp. 931-938
    • Cottone, G.1    Cordone, L.2    Ciccotti, G.3
  • 19
    • 0001965163 scopus 로고    scopus 로고
    • Inhibition of A substates interconversion in trehalose coated carbonmonoxymyoglobin
    • H. Frauenfelder, G. Hummer, and R. Garcia, editors. AIP American Institute of Physics, Melville, NY
    • Librizzi, F., E. Vitrano, and L. Cordone. 1999. Inhibition of A substates interconversion in trehalose coated carbonmonoxymyoglobin. In Biological Physics. H. Frauenfelder, G. Hummer, and R. Garcia, editors. AIP American Institute of Physics, Melville, NY. 132-138.
    • (1999) Biological Physics , pp. 132-138
    • Librizzi, F.1    Vitrano, E.2    Cordone, L.3
  • 20
    • 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
    • Librizzi, F., C. Viappiani, S. Abbruzzetti, and L. Cordone. 2002. 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. 116:1193-1200.
    • (2002) J. Chem. Phys , vol.116 , pp. 1193-1200
    • Librizzi, F.1    Viappiani, C.2    Abbruzzetti, S.3    Cordone, L.4
  • 21
    • 0344984273 scopus 로고    scopus 로고
    • Coupling between the thermal evolution of the heme pocket and the external matrix structure in trehalose coated carboxymyoglobin
    • Giuffrida, S., G. Cottone, F. Librizzi, and L. Cordone. 2003. Coupling between the thermal evolution of the heme pocket and the external matrix structure in trehalose coated carboxymyoglobin. J. Phys. Chem. B. 107:13211-13217.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 13211-13217
    • Giuffrida, S.1    Cottone, G.2    Librizzi, F.3    Cordone, L.4
  • 22
    • 6344281045 scopus 로고    scopus 로고
    • Structure-dynamics coupling between protein and external matrix in sucrose-coated and in trehalose-coated MbCO: An FTIR study
    • Giuffrida, S., G. Cottone, and L. Cordone. 2004. Structure-dynamics coupling between protein and external matrix in sucrose-coated and in trehalose-coated MbCO: an FTIR study. J. Phys. Chem. B. 108:15415-15421.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 15415-15421
    • Giuffrida, S.1    Cottone, G.2    Cordone, L.3
  • 24
    • 33746689781 scopus 로고    scopus 로고
    • Role of solvent on protein-matrix coupling in MbCO embedded in water-saccharide systems: An FTIR study
    • Giuffrida, S., G. Cottone, and L. Cordone. 2006. Role of solvent on protein-matrix coupling in MbCO embedded in water-saccharide systems: an FTIR study. Biophys. J. 91:968-980.
    • (2006) Biophys. J , vol.91 , pp. 968-980
    • Giuffrida, S.1    Cottone, G.2    Cordone, L.3
  • 25
    • 0036902487 scopus 로고    scopus 로고
    • Protein-trehalose-water structures in trehalose coated carboxy-myoglobin
    • Cottone, G., G. Ciccotti, and L. Cordone. 2002. Protein-trehalose-water structures in trehalose coated carboxy-myoglobin. J. Chem. Phys. 117:9862-9866.
    • (2002) J. Chem. Phys , vol.117 , pp. 9862-9866
    • Cottone, G.1    Ciccotti, G.2    Cordone, L.3
  • 26
    • 16344396586 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin
    • Cottone, G., S. Giuffrida, G. Ciccotti, and L. Cordone. 2005. Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin. Proteins. 59:291-302.
    • (2005) Proteins , vol.59 , pp. 291-302
    • Cottone, G.1    Giuffrida, S.2    Ciccotti, G.3    Cordone, L.4
  • 27
    • 27144554035 scopus 로고    scopus 로고
    • Light-induced protein-matrix uncoupling and protein relaxation in dry samples of trehalose-coated MbCO at room temperature
    • Abbruzzetti, S., S. Giuffrida, S. Sottini, C. Viappiani, and L. Cordone. 2005. Light-induced protein-matrix uncoupling and protein relaxation in dry samples of trehalose-coated MbCO at room temperature. Cell Biochem. Biophys. 43:431-438.
    • (2005) Cell Biochem. Biophys , vol.43 , pp. 431-438
    • Abbruzzetti, S.1    Giuffrida, S.2    Sottini, S.3    Viappiani, C.4    Cordone, L.5
  • 28
    • 0037420326 scopus 로고    scopus 로고
    • Motions of single molecules and proteins in trehalose glass
    • Mei, E., J. Tang, J. M. Vanderkooi, and J. M. Hochstrasser. 2003. Motions of single molecules and proteins in trehalose glass. J. Am. Chem. Soc. 125:2730-2735.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 2730-2735
    • Mei, E.1    Tang, J.2    Vanderkooi, J.M.3    Hochstrasser, J.M.4
  • 29
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P., R. H. Valdivia, and S. Falkow. 1996. FACS-optimized mutants of the green fluorescent protein (GFP). Gene. 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 31
    • 0019892005 scopus 로고
    • Renaturation of Aequorea green-fluorescent protein
    • Bokman, S. H., and W. W. Ward. 1981. Renaturation of Aequorea green-fluorescent protein. Biochem. Biophys. Res. Commun. 101:1372-1380.
    • (1981) Biochem. Biophys. Res. Commun , vol.101 , pp. 1372-1380
    • Bokman, S.H.1    Ward, W.W.2
  • 32
    • 84985493765 scopus 로고
    • Spectrophotometric identity of the energy transfer chromophores in Renilla and Aequorea green-fluorescent proteins
    • Ward, W. W., C. W. Cody, R. C. Hart, and M. J. Cormier. 1980. Spectrophotometric identity of the energy transfer chromophores in Renilla and Aequorea green-fluorescent proteins. Photochem. Photobiol. 31:611-615.
    • (1980) Photochem. Photobiol , vol.31 , pp. 611-615
    • Ward, W.W.1    Cody, C.W.2    Hart, R.C.3    Cormier, M.J.4
  • 33
    • 0020482348 scopus 로고
    • Reversible denaturation of Aequorea green-fluorescent protein: Physical separation and characterization of the renatured protein
    • Ward, W. W., and S. H. Bokman. 1982. Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein. Biochemistry. 21:4535-4540.
    • (1982) Biochemistry , vol.21 , pp. 4535-4540
    • Ward, W.W.1    Bokman, S.H.2
  • 35
    • 0028117391 scopus 로고
    • Construction of an overproduction vector containing the novel srp (sterically repressed) promoter
    • Ezaz-Nikpay, K., K. Uchino, R. E. Lerner, and G. L. Verdine. 1994. Construction of an overproduction vector containing the novel srp (sterically repressed) promoter. Protein Sci. 3:132-138.
    • (1994) Protein Sci , vol.3 , pp. 132-138
    • Ezaz-Nikpay, K.1    Uchino, K.2    Lerner, R.E.3    Verdine, G.L.4
  • 36
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P., R. H. Valdivia, and S. Falkow. 1996. FACS-optimized mutants of the green fluorescent protein (GFP). Gene. 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 37
    • 0036231395 scopus 로고    scopus 로고
    • Dynamics of green fluorescent protein mutant2 in solution, on spin-coated glasses, and encapsulated in wet silica gels
    • Chirico, G., F. Cannone, S. Beretta, A. Diaspro, B. Campanini, S. Bettati, R. Ruotolo, and A. Mozzarelli. 2002. Dynamics of green fluorescent protein mutant2 in solution, on spin-coated glasses, and encapsulated in wet silica gels. Protein Sci. 11:1152-1161.
    • (2002) Protein Sci , vol.11 , pp. 1152-1161
    • Chirico, G.1    Cannone, F.2    Beretta, S.3    Diaspro, A.4    Campanini, B.5    Bettati, S.6    Ruotolo, R.7    Mozzarelli, A.8
  • 38
    • 0038529808 scopus 로고    scopus 로고
    • Measurement of the laser pulse width on the microscope objective plane by modulated autocorrelation method
    • Cannone, F., G. Chirico, G. Baldini, and A. Diaspro. 2003. Measurement of the laser pulse width on the microscope objective plane by modulated autocorrelation method. J. Microsc. 210:149-157.
    • (2003) J. Microsc , vol.210 , pp. 149-157
    • Cannone, F.1    Chirico, G.2    Baldini, G.3    Diaspro, A.4
  • 39
  • 41
    • 0036231395 scopus 로고    scopus 로고
    • Dynamics of green fluorescent protein mutant2 in solution, on spin-coated glasses, and encapsulated in wet silica gels
    • Chirico, G., F. Cannone, S. Beretta, A. Diaspro, B. Campanini, S. Bettati, R. Ruotolo, and A. Mozzarelli. 2002. Dynamics of green fluorescent protein mutant2 in solution, on spin-coated glasses, and encapsulated in wet silica gels. Protein Sci. 11:1152-1161.
    • (2002) Protein Sci , vol.11 , pp. 1152-1161
    • Chirico, G.1    Cannone, F.2    Beretta, S.3    Diaspro, A.4    Campanini, B.5    Bettati, S.6    Ruotolo, R.7    Mozzarelli, A.8
  • 42
    • 0043201297 scopus 로고    scopus 로고
    • Single molecule photodynamics by means of one- and two-photon approach
    • Chirico, G., F. Cannone, and A. Diaspro. 2003. Single molecule photodynamics by means of one- and two-photon approach. J. Phys. D: Appl. Phys. 36:1682-1688.
    • (2003) J. Phys. D: Appl. Phys , vol.36 , pp. 1682-1688
    • Chirico, G.1    Cannone, F.2    Diaspro, A.3
  • 43
    • 14144252474 scopus 로고    scopus 로고
    • Single molecule spectroscopic characterization of GFP-MUT2 mutant for two-photon microscopy applications
    • Cannone, F., M. Caccia, S. Bologna, A. Diaspro, and G. Chirico. 2004. Single molecule spectroscopic characterization of GFP-MUT2 mutant for two-photon microscopy applications. Microsc. Res. Tech. 65:186-193.
    • (2004) Microsc. Res. Tech , vol.65 , pp. 186-193
    • Cannone, F.1    Caccia, M.2    Bologna, S.3    Diaspro, A.4    Chirico, G.5
  • 44
    • 0037215718 scopus 로고    scopus 로고
    • Two-photon thermal bleaching of single fluorescent molecules
    • Chirico, G., F. Cannone, G. Baldini, and A. Diaspro. 2003. Two-photon thermal bleaching of single fluorescent molecules. Biophys. J. 84:588-598.
    • (2003) Biophys. J , vol.84 , pp. 588-598
    • Chirico, G.1    Cannone, F.2    Baldini, G.3    Diaspro, A.4
  • 45
    • 1842479439 scopus 로고    scopus 로고
    • Photobleaching of rhodamine 6G in poly(vinyl alcohol) at the ensemble and single-molecule levels
    • Zondervan, R., F. Kulzer, M. A. Kol'chenko, and M. Orrit. 2004. Photobleaching of rhodamine 6G in poly(vinyl alcohol) at the ensemble and single-molecule levels. J. Phys. Chem. A. 108:1657-1665.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 1657-1665
    • Zondervan, R.1    Kulzer, F.2    Kol'chenko, M.A.3    Orrit, M.4
  • 48
    • 0035678612 scopus 로고    scopus 로고
    • Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two-photon excitation
    • Dittrich, P. S., and P. Schwille. 2001. Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two-photon excitation. Appl. Phys. B. 73:829-837.
    • (2001) Appl. Phys. B , vol.73 , pp. 829-837
    • Dittrich, P.S.1    Schwille, P.2
  • 49
    • 0001468698 scopus 로고    scopus 로고
    • Optical studies of single molecules at room temperature
    • Xie, X. S., and J. K. Trautman. 1998. Optical studies of single molecules at room temperature. Annu. Rev. Phys. Chem. 49:441-480.
    • (1998) Annu. Rev. Phys. Chem , vol.49 , pp. 441-480
    • Xie, X.S.1    Trautman, J.K.2
  • 50
    • 0034110795 scopus 로고    scopus 로고
    • Photobleaching in two-photon excitation microscopy
    • Patterson, G. H., and D. W. Piston. 2000. Photobleaching in two-photon excitation microscopy. Biophys. J. 78:2159-2162.
    • (2000) Biophys. J , vol.78 , pp. 2159-2162
    • Patterson, G.H.1    Piston, D.W.2
  • 51
    • 85030511175 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 52
    • 12944303112 scopus 로고    scopus 로고
    • Abbruzzetti, S., E. Grandi, C. Viappiani, S. Bologna, B. Campanini, S. Raboni, S. Bettati, and A. Mozzarelli. 2005. Kinetics of acid-induced spectral changes in the GFPmut2 chromophore. J. Am. Chem. Soc. 127:626-635.
    • Abbruzzetti, S., E. Grandi, C. Viappiani, S. Bologna, B. Campanini, S. Raboni, S. Bettati, and A. Mozzarelli. 2005. Kinetics of acid-induced spectral changes in the GFPmut2 chromophore. J. Am. Chem. Soc. 127:626-635.
  • 53
    • 0002064735 scopus 로고    scopus 로고
    • Single-molecule spectroscopy with 27 fs pulses: Time-resolved experiments and direct imaging of orientational distributions
    • Bopp, N. A., Y. Jia, G. Haran, A. Morlino, and R. M. Hochstrasser. 1998. Single-molecule spectroscopy with 27 fs pulses: time-resolved experiments and direct imaging of orientational distributions. Appl. Phys. Lett. 73:7-9.
    • (1998) Appl. Phys. Lett , vol.73 , pp. 7-9
    • Bopp, N.A.1    Jia, Y.2    Haran, G.3    Morlino, A.4    Hochstrasser, R.M.5
  • 54
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior
    • Zimmer, M. 2002. Green fluorescent protein (GFP): applications, structure, and related photophysical behavior. Chem. Rev. 102:759-781.
    • (2002) Chem. Rev , vol.102 , pp. 759-781
    • Zimmer, M.1
  • 55
    • 0035949666 scopus 로고    scopus 로고
    • On the nature of a glassy state of matter in a hydrated protein: Relation to protein function
    • Teeter, M. M., A. Yamano, B. Stec, and U. Mohanty. 2001. On the nature of a glassy state of matter in a hydrated protein: relation to protein function. Proc. Natl. Acad. Sci. USA. 98:11242-11247.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11242-11247
    • Teeter, M.M.1    Yamano, A.2    Stec, B.3    Mohanty, U.4
  • 56
    • 0002055106 scopus 로고    scopus 로고
    • Spatially heterogeneous dynamics in supercooled liquids
    • Ediger, M. D. 2000. Spatially heterogeneous dynamics in supercooled liquids. Annu. Rev. Phys. Chem. 51:99-128.
    • (2000) Annu. Rev. Phys. Chem , vol.51 , pp. 99-128
    • Ediger, M.D.1
  • 57
    • 0000011127 scopus 로고    scopus 로고
    • Structure and dynamics in concentrated, amorphous carbohydrate-water systems by molecular dynamics simulation
    • Roberts, C. J., and P. G. Debenedetti. 1999. Structure and dynamics in concentrated, amorphous carbohydrate-water systems by molecular dynamics simulation. J. Phys. Chem. B. 103:7308-7318.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 7308-7318
    • Roberts, C.J.1    Debenedetti, P.G.2
  • 58
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • Talaga, D. S., W. L. Lau, H. Roder, J. Tang, Y. Jia, W. F. DeGrado, and R. M. Hochstrasser. 2000. Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl. Acad. Sci. USA. 97:13021-13026.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13021-13026
    • Talaga, D.S.1    Lau, W.L.2    Roder, H.3    Tang, J.4    Jia, Y.5    DeGrado, W.F.6    Hochstrasser, R.M.7


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