메뉴 건너뛰기




Volumn 281, Issue 4, 2014, Pages 1181-1195

The effect of triple glutamic mutations E9Q/E194Q/E204Q on the structural stability of bacteriorhodopsin

Author keywords

conformational changes; hydrogen bonding; molecular dynamics; thermal difference spectra; thermal stability

Indexed keywords

BACTERIORHODOPSIN; GLUTAMINE;

EID: 84894253865     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12694     Document Type: Article
Times cited : (4)

References (67)
  • 2
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • Haupts U, Tittor J, &, Oesterhelt D, (1999) Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu Rev Biophys Biomol Struct 28, 367-399.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 4
    • 69249098842 scopus 로고    scopus 로고
    • Structural snapshots of conformational changes in a seven-helix membrane protein: Lessons from bacteriorhodopsin
    • Hirai T, Subramaniam S, &, Lanyi JK, (2009) Structural snapshots of conformational changes in a seven-helix membrane protein: lessons from bacteriorhodopsin. Curr Opin Struct Biol 19, 433-439.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 433-439
    • Hirai, T.1    Subramaniam, S.2    Lanyi, J.K.3
  • 5
    • 0024325044 scopus 로고
    • A defective proton pump, point-mutated bacteriorhodopsin Asp96-Asn is fully reactivated by azide
    • Tittor J, Soell C, Oesterhelt D, Butt HJ, &, Bamberg E, (1989) A defective proton pump, point-mutated bacteriorhodopsin Asp96-Asn is fully reactivated by azide. EMBO J 8, 3477-3482.
    • (1989) EMBO J , vol.8 , pp. 3477-3482
    • Tittor, J.1    Soell, C.2    Oesterhelt, D.3    Butt, H.J.4    Bamberg, E.5
  • 6
    • 0024024413 scopus 로고
    • Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
    • Mogi T, Stern LJ, Marti T, Chao BH, &, Khorana HG, (1988) Aspartic acid subitutions affect proton translocation by bacteriorhodopsin. ProcNatl Acad Sci USA 85, 4148-4152.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4148-4152
    • Mogi, T.1    Stern, L.J.2    Marti, T.3    Chao, B.H.4    Khorana, H.G.5
  • 7
    • 14844347271 scopus 로고    scopus 로고
    • Proton binding within a membrane protein by a protonated water cluster
    • Garczarek F, Brown LS, Lanyi JK, &, Gerwert K, (2005) Proton binding within a membrane protein by a protonated water cluster. Proc Natl Acad Sci USA 102, 3633-3638.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3633-3638
    • Garczarek, F.1    Brown, L.S.2    Lanyi, J.K.3    Gerwert, K.4
  • 10
    • 0000562142 scopus 로고    scopus 로고
    • Bacteriorhodopsin as a photochromic retinal protein for optical memories
    • Hampp N, (2000) Bacteriorhodopsin as a photochromic retinal protein for optical memories. Chem Rev 100, 1755-1776.
    • (2000) Chem Rev , vol.100 , pp. 1755-1776
    • Hampp, N.1
  • 13
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • Dioumaev AK, Richter HT, Brown LS, Tanio M, Tuzi S, Saito H, Kimura Y, Needleman R, &, Lanyi JK, (1998) Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry 37, 2496-2506.
    • (1998) Biochemistry , vol.37 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saito, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 14
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • Brown LS, Sasaki J, Kandori H, Maeda A, Needleman R, &, Lanyi JK, (1995) Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J Biol Chem 270, 27122-27126.
    • (1995) J Biol Chem , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 15
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • Garczarek F, &, Gerwert K, (2006) Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy. Nature 439, 109-112.
    • (2006) Nature , vol.439 , pp. 109-112
    • Garczarek, F.1    Gerwert, K.2
  • 16
    • 58149376459 scopus 로고    scopus 로고
    • Amino acids with an intermolecular proton bond as proton storage site in bacteriorhodopsin
    • Phatak P, Ghosh N, Yub H, Cuib Q, &, Elstner M, (2008) Amino acids with an intermolecular proton bond as proton storage site in bacteriorhodopsin. Proc Natl Acad Sci USA 105, 19672-19677.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19672-19677
    • Phatak, P.1    Ghosh, N.2    Yub, H.3    Cuib, Q.4    Elstner, M.5
  • 17
    • 0034029916 scopus 로고    scopus 로고
    • Fourier transform infrared evidence for early deprotonation of Asp(85) at alkaline pH in the photocycle of bacteriorhodopsin mutants containing E194Q
    • Lazarova T, Sanz C, Querol E, &, Padrós E, (2000) Fourier transform infrared evidence for early deprotonation of Asp(85) at alkaline pH in the photocycle of bacteriorhodopsin mutants containing E194Q. Biophys J 78, 2022-2030.
    • (2000) Biophys J , vol.78 , pp. 2022-2030
    • Lazarova, T.1    Sanz, C.2    Querol, E.3    Padrós, E.4
  • 18
    • 0037172777 scopus 로고    scopus 로고
    • Specific effects of chloride on the photocycle of E194Q and E204Q mutants of bacteriorhodopsin as measured by FTIR spectroscopy
    • Lazarova T, Sanz C, Sepulcre F, Querol E, &, Padrós E, (2002) Specific effects of chloride on the photocycle of E194Q and E204Q mutants of bacteriorhodopsin as measured by FTIR spectroscopy. Biochemistry 41, 8176-8183.
    • (2002) Biochemistry , vol.41 , pp. 8176-8183
    • Lazarova, T.1    Sanz, C.2    Sepulcre, F.3    Querol, E.4    Padrós, E.5
  • 19
    • 60849083834 scopus 로고    scopus 로고
    • Coupling between the retinal thermal isomerization and the Glu194 residue of bacteriorhodopsin
    • Lazarova T, Querol E, &, Padrós E, (2009) Coupling between the retinal thermal isomerization and the Glu194 residue of bacteriorhodopsin. Photochem Photobiol 85, 617-623.
    • (2009) Photochem Photobiol , vol.85 , pp. 617-623
    • Lazarova, T.1    Querol, E.2    Padrós, E.3
  • 23
    • 2342460436 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • Lanyi JK, (2004) Bacteriorhodopsin. Annu Rev Physiol 66, 665-688.
    • (2004) Annu Rev Physiol , vol.66 , pp. 665-688
    • Lanyi, J.K.1
  • 24
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White S, &, Wimley W, (1999) Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 28, 319-365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.1    Wimley, W.2
  • 25
    • 0029943869 scopus 로고    scopus 로고
    • Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin
    • Booth PJ, Farooq A, &, Flitsch SL, (1996) Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin. Biochemistry 35, 5902-5909.
    • (1996) Biochemistry , vol.35 , pp. 5902-5909
    • Booth, P.J.1    Farooq, A.2    Flitsch, S.L.3
  • 26
    • 0025740089 scopus 로고
    • Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH: Origin of the parallel photocycles of trans-bacteriorhodopsin
    • Balashov SP, Govindjee R, &, Ebrey TG, (1991) Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH: origin of the parallel photocycles of trans-bacteriorhodopsin. Biophys J 60, 475-490.
    • (1991) Biophys J , vol.60 , pp. 475-490
    • Balashov, S.P.1    Govindjee, R.2    Ebrey, T.G.3
  • 27
    • 0029845351 scopus 로고    scopus 로고
    • Evidence that aspartate-85 has a higher pK(a) in all-trans than in 13-cisbacteriorhodopsin
    • Balashov SP, Imasheva ES, Govindjee R, Sheves M, &, Ebrey TG, (1996) Evidence that aspartate-85 has a higher pK(a) in all-trans than in 13-cisbacteriorhodopsin. Biophys J 71, 1973-1984.
    • (1996) Biophys J , vol.71 , pp. 1973-1984
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Sheves, M.4    Ebrey, T.G.5
  • 28
    • 0031013660 scopus 로고    scopus 로고
    • Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; Guanidine hydrochloride restores it
    • Govindjee R, Imasheva ES, Misra S, Balashov SP, Ebrey TG, Chen N, Menick DR, &, Crouch RK, (1997) Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it. Biophys J 72, 886-898.
    • (1997) Biophys J , vol.72 , pp. 886-898
    • Govindjee, R.1    Imasheva, E.S.2    Misra, S.3    Balashov, S.P.4    Ebrey, T.G.5    Chen, N.6    Menick, D.R.7    Crouch, R.K.8
  • 29
    • 0035798539 scopus 로고    scopus 로고
    • Contribution of extracellular Glu residues to the structure and function of bacteriorhodopsin. Presence of specific cation-binding sites
    • Sanz C, Márquez M, Perálvarez A, Elouatik S, Sepulcre F, Querol E, Lazarova T, &, Padrós E, (2001) Contribution of extracellular Glu residues to the structure and function of bacteriorhodopsin. Presence of specific cation-binding sites. J Biol Chem 276, 40788-40794.
    • (2001) J Biol Chem , vol.276 , pp. 40788-40794
    • Sanz, C.1    Márquez, M.2    Perálvarez, A.3    Elouatik, S.4    Sepulcre, F.5    Querol, E.6    Lazarova, T.7    Padrós, E.8
  • 31
    • 0030904764 scopus 로고    scopus 로고
    • Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy
    • Booth PJ, &, Farooq A, (1997) Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy. Eur J Biochem 246, 674-680.
    • (1997) Eur J Biochem , vol.246 , pp. 674-680
    • Booth, P.J.1    Farooq, A.2
  • 33
    • 0008697308 scopus 로고
    • Is the purple color of bacteriorhodopsin maintained by lipid-protein interactions?
    • Baribeau J, &, Boucher F, (1987) Is the purple color of bacteriorhodopsin maintained by lipid-protein interactions? Biochim Biophys Acta 890, 275-278.
    • (1987) Biochim Biophys Acta , vol.890 , pp. 275-278
    • Baribeau, J.1    Boucher, F.2
  • 34
    • 36849090047 scopus 로고    scopus 로고
    • Structural change of bacteriorhodopsin in the purple membrane above pH 10 decreases heterogeneity of the irreversible photobleaching components
    • Yokoyama Y, Sonoyama M, Nakano T, &, Mitaku S, (2007) Structural change of bacteriorhodopsin in the purple membrane above pH 10 decreases heterogeneity of the irreversible photobleaching components. J Biochem 142, 325-333.
    • (2007) J Biochem , vol.142 , pp. 325-333
    • Yokoyama, Y.1    Sonoyama, M.2    Nakano, T.3    Mitaku, S.4
  • 35
    • 0035797895 scopus 로고    scopus 로고
    • Effect of temperature, pH, and metal ion binding on the secondary structure of bacteriorhodopsin: FT-IR study of the melting and premelting transition temperatures
    • Heyes CD, &, El-Sayed MA, (2001) Effect of temperature, pH, and metal ion binding on the secondary structure of bacteriorhodopsin: FT-IR study of the melting and premelting transition temperatures. Biochemistry 40, 11819-11827.
    • (2001) Biochemistry , vol.40 , pp. 11819-11827
    • Heyes, C.D.1    El-Sayed, M.A.2
  • 36
    • 0030455578 scopus 로고    scopus 로고
    • Scanning calorimetry and Fourier-transform infrared studies into the thermal stability of cleaved bacteriorhodopsin systems
    • Azuaga AI, Sepulcre F, Padrós E, &, Mateo PL, (1996) Scanning calorimetry and Fourier-transform infrared studies into the thermal stability of cleaved bacteriorhodopsin systems. Biochemistry 35, 16328-16335.
    • (1996) Biochemistry , vol.35 , pp. 16328-16335
    • Azuaga, A.I.1    Sepulcre, F.2    Padrós, E.3    Mateo, P.L.4
  • 37
    • 0037119403 scopus 로고    scopus 로고
    • The role of the native lipids and lattice structure in bacteriorhodopsin protein conformation and stability as studied by temperature-dependent Fourier transform-infrared spectroscopy
    • Heyes CD, &, El-Sayed MA, (2002) The role of the native lipids and lattice structure in bacteriorhodopsin protein conformation and stability as studied by temperature-dependent Fourier transform-infrared spectroscopy. J Biol Chem 277, 29437-29443.
    • (2002) J Biol Chem , vol.277 , pp. 29437-29443
    • Heyes, C.D.1    El-Sayed, M.A.2
  • 38
    • 0029032977 scopus 로고
    • A pathway for the thermal destabilization of bacteriorhodopsin
    • Taneva SG, Caaveiro JMM, Muga A, &, Goni FM, (1995) A pathway for the thermal destabilization of bacteriorhodopsin. FEBS Lett 367, 297-300.
    • (1995) FEBS Lett , vol.367 , pp. 297-300
    • Taneva, S.G.1    Caaveiro, J.M.M.2    Muga, A.3    Goni, F.M.4
  • 40
    • 0028918705 scopus 로고
    • Spectroscopic studies of bacteriorhodopsin fragments dissolved in organic solution
    • Torres J, &, Padrós E, (1995) Spectroscopic studies of bacteriorhodopsin fragments dissolved in organic solution. Biophys J 68, 2049-2055.
    • (1995) Biophys J , vol.68 , pp. 2049-2055
    • Torres, J.1    Padrós, E.2
  • 41
    • 0018125461 scopus 로고
    • Phase behavior of lipids from Halobacterium halobium
    • Jackson MB, &, Sturtevant JM, (1978) Phase behavior of lipids from Halobacterium halobium. Biochemistry 17, 4470-4474.
    • (1978) Biochemistry , vol.17 , pp. 4470-4474
    • Jackson, M.B.1    Sturtevant, J.M.2
  • 42
    • 0002097215 scopus 로고
    • Phase transitions of the purple membrane and the brown holo-membrane. X-ray diffraction, circular dichroism spectrum and absorption spectrum studies
    • Hiraki K, Hamanaka T, Mitsui T, &, Kito Y, (1981) Phase transitions of the purple membrane and the brown holo-membrane. X-ray diffraction, circular dichroism spectrum and absorption spectrum studies. Biochim Biophys Acta 647, 18-28.
    • (1981) Biochim Biophys Acta , vol.647 , pp. 18-28
    • Hiraki, K.1    Hamanaka, T.2    Mitsui, T.3    Kito, Y.4
  • 44
    • 0023658628 scopus 로고
    • PH dependence of bacteriorhodopsin thermal unfolding
    • Brouillette CG, Muccio DD, &, Finney TK, (1987) pH dependence of bacteriorhodopsin thermal unfolding. Biochemistry 26, 7431-7438.
    • (1987) Biochemistry , vol.26 , pp. 7431-7438
    • Brouillette, C.G.1    Muccio, D.D.2    Finney, T.K.3
  • 45
    • 0028243053 scopus 로고
    • Thermal stability of lipid-depleted purple membranes at neutral and low pH values
    • Taneva SG, Koynova R, &, Tenchov B, (1994) Thermal stability of lipid-depleted purple membranes at neutral and low pH values. FEBS Lett 345, 154-158.
    • (1994) FEBS Lett , vol.345 , pp. 154-158
    • Taneva, S.G.1    Koynova, R.2    Tenchov, B.3
  • 46
    • 0034734243 scopus 로고    scopus 로고
    • Structural determinants of purple membrane assembly
    • Krebs MP, &, Isenbarger TA, (2000) Structural determinants of purple membrane assembly. Biochim Biophys Acta 1460, 15-26.
    • (2000) Biochim Biophys Acta , vol.1460 , pp. 15-26
    • Krebs, M.P.1    Isenbarger, T.A.2
  • 47
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L, Siegert R, Lehmann WD, &, Oesterhelt D, (1998) Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc Natl Acad Sci USA 95, 11673-11678.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 48
    • 0034033871 scopus 로고    scopus 로고
    • The effect of protein conformation change from alpha(II) to alpha(I) on the bacteriorhodopsin photocycle
    • Wang J, &, El-Sayed MA, (2000) The effect of protein conformation change from alpha(II) to alpha(I) on the bacteriorhodopsin photocycle. Biophys J 78, 2031-2036.
    • (2000) Biophys J , vol.78 , pp. 2031-2036
    • Wang, J.1    El-Sayed, M.A.2
  • 49
    • 0029561457 scopus 로고
    • Conformational changes in bacteriorhodopsin associated with protein-protein interactions: A functional alpha I-alpha II helix switch?
    • Torres J, Sepulcre F, &, Padrós E, (1995) Conformational changes in bacteriorhodopsin associated with protein-protein interactions: a functional alpha I-alpha II helix switch? Biochemistry 34, 16320-16326.
    • (1995) Biochemistry , vol.34 , pp. 16320-16326
    • Torres, J.1    Sepulcre, F.2    Padrós, E.3
  • 50
    • 0027526117 scopus 로고
    • The secondary structure of bacteriorhodopsin in organic solution: A Fourier transform infrared study
    • Torres J, &, Padrós E, (1993) The secondary structure of bacteriorhodopsin in organic solution: a Fourier transform infrared study. FEBS Lett 318, 77-79.
    • (1993) FEBS Lett , vol.318 , pp. 77-79
    • Torres, J.1    Padrós, E.2
  • 51
    • 22544465841 scopus 로고    scopus 로고
    • Crystal structures of acid blue and alkaline purple forms of bacteriorhodopsin
    • Okumura H, Murakami M, &, Kouyama T, (2005) Crystal structures of acid blue and alkaline purple forms of bacteriorhodopsin. J Mol Biol 351, 481-495.
    • (2005) J Mol Biol , vol.351 , pp. 481-495
    • Okumura, H.1    Murakami, M.2    Kouyama, T.3
  • 52
    • 1542315401 scopus 로고    scopus 로고
    • Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determinants for conformation and dynamics as revealed by site-directed solid-state 13C NMR
    • Saito H, Yamaguchi S, Ogawa K, Tuzi S, Márquez M, Sanz C, &, Padrós E, (2004) Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determinants for conformation and dynamics as revealed by site-directed solid-state 13C NMR. Biophys J 86, 1673-1681.
    • (2004) Biophys J , vol.86 , pp. 1673-1681
    • Saito, H.1    Yamaguchi, S.2    Ogawa, K.3    Tuzi, S.4    Márquez, M.5    Sanz, C.6    Padrós, E.7
  • 53
    • 48649083203 scopus 로고    scopus 로고
    • Role of extracellular glutamic acids in the stability and energy landscape of bacteriorhodopsin
    • Sapra KT, Doehner J, Renugopalakrishnan V, Padrós E, &, Muller DJ, (2008) Role of extracellular glutamic acids in the stability and energy landscape of bacteriorhodopsin. Biophys J 95, 3407-3418.
    • (2008) Biophys J , vol.95 , pp. 3407-3418
    • Sapra, K.T.1    Doehner, J.2    Renugopalakrishnan, V.3    Padrós, E.4    Muller, D.J.5
  • 54
    • 0034607683 scopus 로고    scopus 로고
    • Evidence for long range allosteric interactions between the extracellular and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C
    • Alexiev U, Mollaaghababa R, Khorana HG, &, Heyn MP, (2000) Evidence for long range allosteric interactions between the extracellular and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C. J Biol Chem 275, 13431-13440.
    • (2000) J Biol Chem , vol.275 , pp. 13431-13440
    • Alexiev, U.1    Mollaaghababa, R.2    Khorana, H.G.3    Heyn, M.P.4
  • 55
    • 0018101534 scopus 로고
    • Intermolecular interactions and anesthesia
    • Sandorfy C, (1978) Intermolecular interactions and anesthesia. Anesthesiology 48, 357-359.
    • (1978) Anesthesiology , vol.48 , pp. 357-359
    • Sandorfy, C.1
  • 56
    • 0024967187 scopus 로고
    • Purple membrane: Color, crystallinity, and the effect of dimethyl sulfoxide
    • Pande C, Callender R, Henderson R, &, Pande A, (1989b) Purple membrane: color, crystallinity, and the effect of dimethyl sulfoxide. Biochemistry 28, 5971-5978.
    • (1989) Biochemistry , vol.28 , pp. 5971-5978
    • Pande, C.1    Callender, R.2    Henderson, R.3    Pande, A.4
  • 57
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D, &, Stoeckenius W, (1974) Isolation of the cell membrane of halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol 31, 667-678.
    • (1974) Methods Enzymol , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 58
    • 0019840442 scopus 로고
    • Thermal denaturation of streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex
    • Takahashi K, &, Sturtevant JM, (1981) Thermal denaturation of streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex. Biochemistry 20, 6185-6190.
    • (1981) Biochemistry , vol.20 , pp. 6185-6190
    • Takahashi, K.1    Sturtevant, J.M.2
  • 60
    • 0032561127 scopus 로고    scopus 로고
    • A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
    • Takeda K, Sato H, Hino T, Kono M, Fukuda K, Sakurai I, Okada T, &, Kouyama T, (1998) A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J Mol Biol 283, 463-474.
    • (1998) J Mol Biol , vol.283 , pp. 463-474
    • Takeda, K.1    Sato, H.2    Hino, T.3    Kono, M.4    Fukuda, K.5    Sakurai, I.6    Okada, T.7    Kouyama, T.8
  • 61
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky T, Nielsen J, McCammon J, &, Baker N, (2004) PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 32, 665-667.
    • (2004) Nucleic Acids Res , vol.32 , pp. 665-667
    • Dolinsky, T.1    Nielsen, J.2    McCammon, J.3    Baker, N.4
  • 63
    • 0034128699 scopus 로고    scopus 로고
    • Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin
    • Tajkhorshid E, Baudry J, Schulten K, &, Suhai S, (2000) Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin. Biophys J 78, 683-693.
    • (2000) Biophys J , vol.78 , pp. 683-693
    • Tajkhorshid, E.1    Baudry, J.2    Schulten, K.3    Suhai, S.4
  • 64
    • 0343155178 scopus 로고    scopus 로고
    • Quantum chemical and free energy simulation analysis of retinal conformational energetics
    • Baudry J, Crouzy S, Roux B, &, Smith JC, (1997) Quantum chemical and free energy simulation analysis of retinal conformational energetics. J Chem Info Comput Sci 37, 1018-1024.
    • (1997) J Chem Info Comput Sci , vol.37 , pp. 1018-1024
    • Baudry, J.1    Crouzy, S.2    Roux, B.3    Smith, J.C.4
  • 65
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, &, Lindahl E, (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4, 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.