메뉴 건너뛰기




Volumn 71, Issue 2, 1996, Pages 670-681

Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: A molecular dynamics free energy perturbation study

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; ION CHANNEL; WATER;

EID: 0029757992     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79267-6     Document Type: Article
Times cited : (250)

References (70)
  • 1
    • 0026612756 scopus 로고
    • a values of ionizable groups in bacteriorhodopsin
    • a values of ionizable groups in bacteriorhodopsin. J. Mol. Biol. 224: 473-486.
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 2
    • 0001655657 scopus 로고
    • Finite representation of an infinite bulk system: Solvent boundary potential for computer simulations
    • Beglov, D., and B. Roux. 1994. Finite representation of an infinite bulk system: solvent boundary potential for computer simulations. J. Chem. Phys. 100:9050-9063.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9050-9063
    • Beglov, D.1    Roux, B.2
  • 3
    • 84989730198 scopus 로고
    • Theoretical study of color control mechanism in retinal proteins. I. Role of the tryptophan residue, tyrosine residue, and water molecule
    • Beppu, Y., and T. Kakitani. 1994. Theoretical study of color control mechanism in retinal proteins. I. Role of the tryptophan residue, tyrosine residue, and water molecule. Photochem. Photobiol. 59(6):660-669.
    • (1994) Photochem. Photobiol. , vol.59 , Issue.6 , pp. 660-669
    • Beppu, Y.1    Kakitani, T.2
  • 4
    • 84989691688 scopus 로고
    • Energetics of protonation-deprotonation of the chromophore in retinal proteins
    • Beppu, Y., T. Katakini, and F. Tokunaga. 1992. Energetics of protonation-deprotonation of the chromophore in retinal proteins. Photochem. Photobiol. 56:1113-1117.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1113-1117
    • Beppu, Y.1    Katakini, T.2    Tokunaga, F.3
  • 5
    • 0027968902 scopus 로고
    • Free energy simulations: The meaning of the individual contributions from a component analysis
    • Boresch, S., G. Archontis, and M. Karplus. 1994. Free energy simulations: the meaning of the individual contributions from a component analysis. Proteins. 20:25-33.
    • (1994) Proteins , vol.20 , pp. 25-33
    • Boresch, S.1    Archontis, G.2    Karplus, M.3
  • 6
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
    • Braiman, M. S., T. Mogi, T. Marti, L. J. Stern, H. G. Khorana, and K. J. Rothschild. 1988. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. Biochemistry. 27:8516-8520.
    • (1988) Biochemistry , vol.27 , pp. 8516-8520
    • Braiman, M.S.1    Mogi, T.2    Marti, T.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 8
    • 0001031179 scopus 로고
    • Proteins: A Theoretical perspective of dynamics structure and thermodynamics
    • 1. Prigogine and S. A. Rice, editors. John Wiley & Sons, New York
    • Brooks, C. L. III, M. Karplus, and B. M. Pettitt. 1988. Proteins: a Theoretical perspective of dynamics structure and thermodynamics. In Advances in Chemical Physics, Vol. LXXI. 1. Prigogine and S. A. Rice, editors. John Wiley & Sons, New York.
    • (1988) Advances in Chemical Physics , vol.71
    • Brooks III, C.L.1    Karplus, M.2    Pettitt, B.M.3
  • 9
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brunger, A. T., and M. Karplus. 1988. Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins. 4:148-156.
    • (1988) Proteins , vol.4 , pp. 148-156
    • Brunger, A.T.1    Karplus, M.2
  • 10
    • 0344335730 scopus 로고
    • Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump
    • Butt, H. J., K. Fendler, E. Bamberg, J. Tittor, and D. Oesterhelt. 1989. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO J. 8:1657-1663.
    • (1989) EMBO J. , vol.8 , pp. 1657-1663
    • Butt, H.J.1    Fendler, K.2    Bamberg, E.3    Tittor, J.4    Oesterhelt, D.5
  • 11
    • 0026332339 scopus 로고
    • Water is required for proton transfer from Asp 96 to the bacteriorhodopsin Schiff base
    • Cao, Y., G. Váró, M. Chang, B. Ni, R. Needleman, and J. K. Lanyi. 1991. Water is required for proton transfer from Asp 96 to the bacteriorhodopsin Schiff base. Biochemistry. 30:10972-10979.
    • (1991) Biochemistry , vol.30 , pp. 10972-10979
    • Cao, Y.1    Váró, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 13
    • 0028266198 scopus 로고
    • Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: A resonance Raman study of the Schiff base hydrogen/deuterium exchange
    • Deng, H., L. Huang, R. Callender, and T. Ebrey. 1994. Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange. Biophys. J. 66:1129-1136.
    • (1994) Biophys. J. , vol.66 , pp. 1129-1136
    • Deng, H.1    Huang, L.2    Callender, R.3    Ebrey, T.4
  • 14
    • 0029081424 scopus 로고
    • Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant
    • Desinov, V. P., B. Halle, J. Peters, and H. D. Horlein. 1995. Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant. Biochemistry. 34:9046-9051.
    • (1995) Biochemistry , vol.34 , pp. 9046-9051
    • Desinov, V.P.1    Halle, B.2    Peters, J.3    Horlein, H.D.4
  • 17
    • 0029026347 scopus 로고
    • Structure and fluctuations of bacteriorhodopsin in the purple membrane: A molecular dynamics study
    • Edholm, O., O. Berger, and F. Jähnig. 1995. Structure and fluctuations of bacteriorhodopsin in the purple membrane: a molecular dynamics study. J. Mol. Biol. 250:94-111.
    • (1995) J. Mol. Biol. , vol.250 , pp. 94-111
    • Edholm, O.1    Berger, O.2    Jähnig, F.3
  • 18
    • 0020861687 scopus 로고
    • Water and proteins. II. The location and dynamics of water in protein systems and its relation to their stability and properties
    • Edsall, J. T., and H. A. McKenzie. 1983. Water and proteins. II. The location and dynamics of water in protein systems and its relation to their stability and properties. Adv. Biophys. 16:53-183.
    • (1983) Adv. Biophys. , vol.16 , pp. 53-183
    • Edsall, J.T.1    McKenzie, H.A.2
  • 20
    • 0027220385 scopus 로고
    • Structure and dynamics of bacteriorhodopsin: Comparison of experiment and simulation
    • Ferrand, M., G. Zaccaï, M. Nina, J. C. Smith, C. Etchebest, and B. Roux. 1993. Structure and dynamics of bacteriorhodopsin: comparison of experiment and simulation. FEBS Lest. 327:256-260.
    • (1993) FEBS Lest. , vol.327 , pp. 256-260
    • Ferrand, M.1    Zaccaï, G.2    Nina, M.3    Smith, J.C.4    Etchebest, C.5    Roux, B.6
  • 21
    • 0028073137 scopus 로고
    • Detection of a water molecule in the active site of bacteriorhodopsin: Hydrogen bonding changes during the primary photoreaction
    • Fischer, W. B., S. Sonar, T. Marti, H. G. Khorana. and K. J. Rothschild. 1994. Detection of a water molecule in the active site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction. Biochemistry. 33:12757-12762.
    • (1994) Biochemistry , vol.33 , pp. 12757-12762
    • Fischer, W.B.1    Sonar, S.2    Marti, T.3    Khorana, H.G.4    Rothschild, K.J.5
  • 22
    • 0000559536 scopus 로고
    • a of the retinal protonated Schiff base in retinal proteins: A study with model compounds
    • a of the retinal protonated Schiff base in retinal proteins: a study with model compounds. J. Am. Chem. Soc. 115:3772-3773.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 23
    • 0023130071 scopus 로고
    • Only water-exposed carboxyl groups are protonated during the transition to the cation-free bacteriorhodopsin
    • Gerwert, K., U. M. Ganter, F. Siebert, and B. Hess. 1987. Only water-exposed carboxyl groups are protonated during the transition to the cation-free bacteriorhodopsin. FEBS Lett. 213:39-44.
    • (1987) FEBS Lett. , vol.213 , pp. 39-44
    • Gerwert, K.1    Ganter, U.M.2    Siebert, F.3    Hess, B.4
  • 24
    • 0024707259 scopus 로고
    • Role of aspartate 96 in proton translocation by bacteriorhodopsin
    • Gerwert, K., B. Hess, J. Soppa, and D. Oesterhelt. 1989. Role of aspartate 96 in proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 86:4943-4947.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4943-4947
    • Gerwert, K.1    Hess, B.2    Soppa, J.3    Oesterhelt, D.4
  • 25
    • 0025629995 scopus 로고
    • Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization. and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy
    • Gerwert, K., G. Souvignier, and B. Hess. 1990. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization. and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy. Proc. Natl. Acad. Sci. USA. 87:9774-9778.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9774-9778
    • Gerwert, K.1    Souvignier, G.2    Hess, B.3
  • 26
    • 33845280969 scopus 로고
    • Solid-state NMR detection of proton exchange between the bacteriorhodopsin Schiff base and bulk water
    • Harbison, G. S., J. E. Roberts, J. Herzfeld, and R. G. Griffin. 1988. Solid-state NMR detection of proton exchange between the bacteriorhodopsin Schiff base and bulk water. J. Am. Chem. Soc. 110:7221-7227.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7221-7227
    • Harbison, G.S.1    Roberts, J.E.2    Herzfeld, J.3    Griffin, R.G.4
  • 29
    • 0029160249 scopus 로고
    • Thermodynamics of water mediating protein-ligand interactions in cylochrome P450cam: A molecular dynamics study
    • Helms, V., and R. C. Wade. 1995. Thermodynamics of water mediating protein-ligand interactions in cylochrome P450cam: a molecular dynamics study. Biophys. J. 69:810-824.
    • (1995) Biophys. J. , vol.69 , pp. 810-824
    • Helms, V.1    Wade, R.C.2
  • 30
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J. Mol. Biol. 213: 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 31
    • 85005687495 scopus 로고
    • The free energy of xenon binding to myoglobin from molecular dynamics simulation
    • Hermans, J., and S. Shankar. 1986. The free energy of xenon binding to myoglobin from molecular dynamics simulation, Isr. J. Chem. 27: 225-227.
    • (1986) Isr. J. Chem. , vol.27 , pp. 225-227
    • Hermans, J.1    Shankar, S.2
  • 33
    • 0000217440 scopus 로고
    • Role of water in bacteriorhodopsin's chromophore: Resonance Raman study
    • Hildebrandt, P., and M. Stockburger. 1984. Role of water in bacteriorhodopsin's chromophore: resonance Raman study. Biochemistry. 23: 5539-5548.
    • (1984) Biochemistry , vol.23 , pp. 5539-5548
    • Hildebrandt, P.1    Stockburger, M.2
  • 34
    • 0024651574 scopus 로고
    • Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement
    • Holz, M., L. A. Drachev, T. Mogi, H. Otto, A. D. Kaulen, M. P. Heyn, V. P. Skulachev, and H. G. Khorana. 1989. Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement. Proc. Natl. Acad. Sci. USA. 86:2167-2171.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2167-2171
    • Holz, M.1    Drachev, L.A.2    Mogi, T.3    Otto, H.4    Kaulen, A.D.5    Heyn, M.P.6    Skulachev, V.P.7    Khorana, H.G.8
  • 35
    • 0028258544 scopus 로고
    • Molecular dynamics study of bacteriorhodopsin and artificial pigments
    • Humphrey, W., I. Logunov, K. Schulten, and M. Sheves. 1994. Molecular dynamics study of bacteriorhodopsin and artificial pigments. Biochemistry. 33:3668-3678.
    • (1994) Biochemistry , vol.33 , pp. 3668-3678
    • Humphrey, W.1    Logunov, I.2    Schulten, K.3    Sheves, M.4
  • 37
    • 33646471468 scopus 로고
    • Statistical mechanics of fluid mixtures
    • Kirkwood, J. G. 1935. Statistical mechanics of fluid mixtures. J. Chem. Phys. 3:300-313.
    • (1935) J. Chem. Phys. , vol.3 , pp. 300-313
    • Kirkwood, J.G.1
  • 38
    • 7044239742 scopus 로고
    • Free energy calculations: Applications to chemical and biochemical phenomena
    • Kollman, P. 1993. Free energy calculations: applications to chemical and biochemical phenomena. Chem. Rev. 93:2395-2417.
    • (1993) Chem. Rev. , vol.93 , pp. 2395-2417
    • Kollman, P.1
  • 39
    • 0018177840 scopus 로고
    • Experimental evidence for secondary protein-chromophore interactions at the Schiff base linkage in bacteriorhodopsin: Molecular mechanism for proton pumping
    • Lewis, A., M. A. Marcus, B. Ehrenberg, and H. Crespi. 1978. Experimental evidence for secondary protein-chromophore interactions at the Schiff base linkage in bacteriorhodopsin: molecular mechanism for proton pumping. Proc. Nat. Acad. Sci. USA. 75:4642-4646.
    • (1978) Proc. Nat. Acad. Sci. USA , vol.75 , pp. 4642-4646
    • Lewis, A.1    Marcus, M.A.2    Ehrenberg, B.3    Crespi, H.4
  • 41
    • 0028279038 scopus 로고
    • Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: A Fourier transform infrared spectroscopic study
    • Maeda, A., J. Sasaki, Y. Yamasaki, R. Needleman, and J. Lanyi. 1994. Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier transform infrared spectroscopic study. Biochemistry. 33:1713-1717.
    • (1994) Biochemistry , vol.33 , pp. 1713-1717
    • Maeda, A.1    Sasaki, J.2    Yamasaki, Y.3    Needleman, R.4    Lanyi, J.5
  • 42
    • 0025873898 scopus 로고
    • Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation
    • Marti, T., H. Otto, T. Mogi, S. J. Rösselet, M. P. Heyn, and H. G. Khorana. 1991. Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation. J. Biol. Chem. 266:6919-6927.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6919-6927
    • Marti, T.1    Otto, H.2    Mogi, T.3    Rösselet, S.J.4    Heyn, M.P.5    Khorana, H.G.6
  • 43
    • 0027082924 scopus 로고
    • Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications
    • Meyer, E. 1992. Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications. Protein Sci. 1:1543-1562.
    • (1992) Protein Sci. , vol.1 , pp. 1543-1562
    • Meyer, E.1
  • 44
    • 0023393593 scopus 로고
    • Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation
    • Mogi, T., L. J. Stern, N. R. Hackett, and H. G. Khorana. 1987. Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation. Proc. Natl. Acat. Sci. USA. 85:5595-5599.
    • (1987) Proc. Natl. Acat. Sci. USA , vol.85 , pp. 5595-5599
    • Mogi, T.1    Stern, L.J.2    Hackett, N.R.3    Khorana, H.G.4
  • 45
    • 85030271147 scopus 로고
    • Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
    • Mogi, T., L. J. Stern, T. Marti, B. H. Chao, and H. G. Khorana. 1988. Aspartic acid substitutions affect proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 84:5595-5599.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5595-5599
    • Mogi, T.1    Stern, L.J.2    Marti, T.3    Chao, B.H.4    Khorana, H.G.5
  • 46
    • 0028835990 scopus 로고
    • Functional interactions in bacteriorhodopsin: A theoretical analysis of retinal hydrogen bonding
    • Nina, M., B. Roux, and J. C. Smith. 1995. Functional interactions in bacteriorhodopsin: a theoretical analysis of retinal hydrogen bonding. Biophys. J. 68:25-39.
    • (1995) Biophys. J. , vol.68 , pp. 25-39
    • Nina, M.1    Roux, B.2    Smith, J.C.3
  • 47
    • 37949037346 scopus 로고
    • Ab initio quantum chemical analysis of water-Schiff base interactions in bacteriorhodopsin
    • Nina, M., J. C. Smith, and B. Roux. 1993. Ab initio quantum chemical analysis of water-Schiff base interactions in bacteriorhodopsin. J. Mol. Struct. 286:231-245.
    • (1993) J. Mol. Struct. , vol.286 , pp. 231-245
    • Nina, M.1    Smith, J.C.2    Roux, B.3
  • 48
    • 84989685275 scopus 로고
    • Structure of bacteriorhodopsin and in situ isomerization of retinal: A molecular dynamics study
    • Nonella, M., A. Windemuth, and K. Schulten. 1991. Structure of bacteriorhodopsin and in situ isomerization of retinal: a molecular dynamics study. Photochem. Photobiol. 54:937-948.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 937-948
    • Nonella, M.1    Windemuth, A.2    Schulten, K.3
  • 49
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D., and W. Stoeckenius. 1971. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol. 233: 149-152.
    • (1971) Nature New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 51
    • 0343791148 scopus 로고
    • Electric moments of molecules in liquids
    • Onsager, L. 1936. Electric moments of molecules in liquids. J. Chem. Phys. 58:1486-1493.
    • (1936) J. Chem. Phys. , vol.58 , pp. 1486-1493
    • Onsager, L.1
  • 52
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • Otto, H., T. Marti, M. Holz, T. Mogi, M. Lindau, H. G. Khorana, and M. P. Heyn. 1989. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 86:9228-9232.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 53
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction
    • Papadopoulos, G., N. Dencher, G. Zaccaï, and G. Büldt. 1990. Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. J. Mol. Biol. 214: 15-19.
    • (1990) J. Mol. Biol. , vol.214 , pp. 15-19
    • Papadopoulos, G.1    Dencher, N.2    Zaccaï, G.3    Büldt, G.4
  • 54
    • 0001060458 scopus 로고
    • A Monte Carlo method for obtaining the interionic potential of mean force in ionic solution
    • Patey, G. N., and J. P. Valleau. 1975. A Monte Carlo method for obtaining the interionic potential of mean force in ionic solution. J. Chem. Phys. 63:2334-2339.
    • (1975) J. Chem. Phys. , vol.63 , pp. 2334-2339
    • Patey, G.N.1    Valleau, J.P.2
  • 55
    • 0026564606 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds
    • Rothschild, K. J., Y.-W. He, S. Sonar, T. Marti, and H. G. Khorana. 1992. Vibrational spectroscopy of bacteriorhodopsin mutants: evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds. J. Biol. Chem. 267:1615-1622.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1615-1622
    • Rothschild, K.J.1    He, Y.-W.2    Sonar, S.3    Marti, T.4    Khorana, H.G.5
  • 56
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equation of motions of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equation of motions of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Chem. 23: 327-341.
    • (1977) J. Comp. Chem. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 57
    • 0028218956 scopus 로고
    • Environmental effects on the protonation states of active site residues in bacteriorhodopsin
    • Sampogna, R. V., and B. Honig. 1994. Environmental effects on the protonation states of active site residues in bacteriorhodopsin. Biophys. J. 66:1341-1352.
    • (1994) Biophys. J. , vol.66 , pp. 1341-1352
    • Sampogna, R.V.1    Honig, B.2
  • 59
    • 0000713081 scopus 로고
    • An approach to the application of free energy perturbation methods using molecular dynamics
    • Singh U. C., F. K. Brown, P. A. Bash, and P. A. Kollman. 1987. An approach to the application of free energy perturbation methods using molecular dynamics. J. Am. Chem. Soc. 109:1607-1614.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 1607-1614
    • Singh, U.C.1    Brown, F.K.2    Bash, P.A.3    Kollman, P.A.4
  • 61
    • 0027303125 scopus 로고
    • Protein catalysis of retinal suhpicosecond photoisomerisation in the primary process of bacteriorhodopsin photosynthesis
    • Song, L., M. A. El-Sayed, and J. K. Lanyi. 1993. Protein catalysis of retinal suhpicosecond photoisomerisation in the primary process of bacteriorhodopsin photosynthesis. Science. 261:891-894.
    • (1993) Science , vol.261 , pp. 891-894
    • Song, L.1    El-Sayed, M.A.2    Lanyi, J.K.3
  • 62
    • 0024978473 scopus 로고
    • Structure-function studies on bacteriorhodopsin: Individual substitutions of Arg residues by Gln affect chromophore formation, photocycle and proton translocation
    • Stern, L. J., and H. G. Khorana. 1989. Structure-function studies on bacteriorhodopsin: individual substitutions of Arg residues by Gln affect chromophore formation, photocycle and proton translocation. J. Biol. Chem. 264:14202-14208.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14202-14208
    • Stern, L.J.1    Khorana, H.G.2
  • 63
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S., M. Gerstein, D. Oesterhelt, and R. Henderson. 1993. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12:1-8.
    • (1993) EMBO J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 64
    • 0025157075 scopus 로고
    • Protonation state of Asp (Glu 85) regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg 82 → Glu: The blue form is inactive in proton translocation
    • Subramaniam, S., T. Marti, and H. G. Khorana. 1990. Protonation state of Asp (Glu 85) regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg 82 → Glu: the blue form is inactive in proton translocation. Proc. Nat. Acad. Sci. USA. 87:1013-1017.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3
  • 65
    • 0005336155 scopus 로고
    • Hydration of cavities in proteins: A molecular dynamics approach
    • Wade, R. C., M. H. Mazor, J. A. McCammon, and F. A. Quiocho. 1990. Hydration of cavities in proteins: a molecular dynamics approach. J. Am. Chem. Soc. 112:7057-7059.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7057-7059
    • Wade, R.C.1    Mazor, M.H.2    McCammon, J.A.3    Quiocho, F.A.4
  • 66
    • 0026189146 scopus 로고
    • A molecular dynamics study of thermodynamic and structural aspects of the hydration of cavities in proteins
    • Wade, R. C., M. H. Mazor, J. A. McCammon, and F. A. Quiocho. 1991. A molecular dynamics study of thermodynamic and structural aspects of the hydration of cavities in proteins. Biopolymers. 31:919-931.
    • (1991) Biopolymers , vol.31 , pp. 919-931
    • Wade, R.C.1    Mazor, M.H.2    McCammon, J.A.3    Quiocho, F.A.4
  • 67
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams, M. A., J. M. Goodfellow, and J. M. Thornton. 1994. Buried waters and internal cavities in monomeric proteins. Protein Sci. 3:1224-1235.
    • (1994) Protein Sci. , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 68
    • 0023644695 scopus 로고
    • Structure and hydration of purple membranes in different conditions
    • Zaccaï, G. 1987. Structure and hydration of purple membranes in different conditions. J. Mol. Biol. 194:569-572.
    • (1987) J. Mol. Biol. , vol.194 , pp. 569-572
    • Zaccaï, G.1
  • 69
    • 36449002336 scopus 로고
    • Separation-shifted scaling, a new scaling method for Lennard-Jones interactions in thermodynamic integration
    • Zacharias, M., T. P. Straatsma, and J. A. McCammon. 1994. Separation-shifted scaling, a new scaling method for Lennard-Jones interactions in thermodynamic integration. J. Chem. Phys. 100:9025-9031.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9025-9031
    • Zacharias, M.1    Straatsma, T.P.2    McCammon, J.A.3
  • 70
    • 0027476774 scopus 로고
    • Molecular dynamics study of the proton pump cycle of bacteriorhodopsin
    • Zhou, F., A. Windemuth, and K. Schulten. 1993. Molecular dynamics study of the proton pump cycle of bacteriorhodopsin. Biochemistry. 32:2291-2306.
    • (1993) Biochemistry , vol.32 , pp. 2291-2306
    • Zhou, F.1    Windemuth, A.2    Schulten, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.