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Volumn 19, Issue 8, 2012, Pages 791-794

Effect of the compatible solute ectoine on the stability of the membrane proteins

Author keywords

Atomic force microscopy; Compatible solutes; Ectoine; Force spectroscopy; Membrane proteins

Indexed keywords

BACTERIORHODOPSIN; ECTOINE;

EID: 84865355673     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986612801619570     Document Type: Article
Times cited : (39)

References (35)
  • 1
    • 0004133430 scopus 로고
    • Microbial water stress physiology
    • 1 ed.; Wiley and Sons: New York
    • Brown, A.D. Microbial water stress physiology. Principles and perspectives, 1 ed.; Wiley and Sons: New York, 1990.
    • (1990) Principles and Perspectives
    • Brown, A.D.1
  • 3
    • 0021799461 scopus 로고
    • 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid a novel cyclic amino acid from halophilic phototrophic bacteria of the genus ectothiorhodospira
    • 135-139
    • Galinski, E.A.; Pfeiffer, H.P.; Trüper, H.G. 1,4,5,6-Tetrahydro-2- methyl-4-pyrimidinecarboxylic acid. A novel cyclic amino acid from halophilic phototrophic bacteria of the genus Ectothiorhodospira. Eur. J. Biochem., 1985, 149, 135-139.
    • (1985) Eur J Biochem , pp. 149
    • Galinski, E.A.1    Pfeiffer, H.P.2    Trüper, H.G.3
  • 4
    • 0028783450 scopus 로고
    • Osmoadaptation in bacteria
    • Galinski, E.A. Osmoadaptation in Bacteria. Adv. Microb. Physiol., 1995, 37, 273-328.
    • (1995) Adv. Microb. Physiol. , vol.37 , pp. 273-328
    • Galinski, E.A.1
  • 5
    • 0033180252 scopus 로고    scopus 로고
    • Extrinsic protein stabilization by the naturally occurring osmolytes β-hydroxyectoine and betaine
    • DOI 10.1007/s007920050116
    • Knapp, S.; Ladenstein, R.; Galinski, E.A. Extrinsic protein stabilization by the naturally occurring osmolytes beta-hydroxyectoine and betaine. Extremophiles, 1999, 3, 191-198. (Pubitemid 29405310)
    • (1999) Extremophiles , vol.3 , Issue.3 , pp. 191-198
    • Knapp, S.1    Ladenstein, R.2    Erwin, A.G.3
  • 8
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P.H.; Clarke, M.E.; Hand, S.C.; Bowlus, R.D.; Somero, G.N. Living with water stress: evolution of osmolyte systems. Science, 1982, 217, 1214-1222. (Pubitemid 13283134)
    • (1982) Science , vol.217 , Issue.4566 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 9
    • 0001855948 scopus 로고
    • A physicochemical basis for the selection of osmolytes by nature
    • Springer-Verlag, Berlin, G.N. Somero, Osmond, C.B.; Bolls, C.L., Eds.
    • Timasheff, S.N. A physicochemical basis for the selection of osmolytes by nature. In: G.N. Somero, Osmond, C.B.; Bolls, C.L., Eds.; Water and life. Springer-Verlag, Berlin, 1992, pp. 70-84.
    • (1992) Water and Life , pp. 70-84
    • Timasheff, S.N.1
  • 10
    • 0035237232 scopus 로고    scopus 로고
    • Protein stabilization by naturally occurring osmolytes
    • Bolen, D.W. Protein stabilization by naturally occurring osmolytes. Methods Mol. Biol., 2001, 168, 17-36.
    • (2001) Methods Mol. Biol. , vol.168 , pp. 17-36
    • Bolen, D.W.1
  • 11
    • 0035703118 scopus 로고    scopus 로고
    • Osmoadaptation in bacteria and archaea: Common principles and differences
    • DOI 10.1046/j.1462-2920.2001.00252.x
    • Roessler, M.; Müller, V. Osmoadaptation in bacteria and archaea: common principles and differences. Environ. Microbiol., 2001, 3, 743-754. (Pubitemid 34103164)
    • (2001) Environmental Microbiology , vol.3 , Issue.12 , pp. 743-754
    • Roessler, M.1    Muller, V.2
  • 12
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T.; Timasheff, S.N. The stabilization of proteins by osmolytes. Biophys. J., 1985, 47, 411- 414.
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 13
    • 0037693029 scopus 로고    scopus 로고
    • Impact of compatible solutes on the mechanical properties of fibronectin: A single molecule analysis
    • Oberdörfer, Y.; Schrot, S.; Fuchs, H.; Galinski, E.A.; Janshoff, A. Impact of compatible solutes on the mechanical properties of fibronectin: a single molecule analysis. PCCP, 2003, 5, 1876-1881.
    • (2003) PCCP , vol.5 , pp. 1876-1881
    • Oberdörfer, Y.1    Schrot, S.2    Fuchs, H.3    Galinski, E.A.4    Janshoff, A.5
  • 14
    • 0039801358 scopus 로고    scopus 로고
    • Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additives
    • DOI 10.1016/S1381-1177(99)00043-0, PII S1381117799000430
    • Göller, K.; Galinski, E.A. Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additives. J. Mol. Catal. B Enzym., 1999, 7, 37-45. (Pubitemid 29408514)
    • (1999) Journal of Molecular Catalysis - B Enzymatic , vol.7 , Issue.1-4 , pp. 37-45
    • Goller, K.1    A. Galinski, E.2
  • 17
    • 0041841000 scopus 로고    scopus 로고
    • Mapping flexible protein domains at subnanometer resolution with the atomic force microscope
    • DOI 10.1016/S0014-5793(98)00623-1, PII S0014579398006231
    • Müller, D.J.; Fotiadis, D.; Engel, A. Mapping flexible protein domains at subnanometer resolution with the atomic force microscope. FEBS Lett., 1998, 430, 105-111. (Pubitemid 28307041)
    • (1998) FEBS Letters , vol.430 , Issue.1-2 , pp. 105-111
    • Muller, D.J.1    Fotiadis, D.2    Engel, A.3
  • 18
    • 0028947257 scopus 로고
    • Funnels pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J.D.; Onuchic, J.N.; Socci, N. D.; Wolynes, P.G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins, 1995, 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 21
    • 0034616309 scopus 로고    scopus 로고
    • Unfolding pathways of individual bacteriorhodopsins
    • DOI 10.1126/science.288.5463.143
    • Oesterhelt, F.; Oesterhelt, D.; Pfeiffer, M.; Engel, A.; Gaub, H.E.; Müller, D.J. Unfolding Pathways of Individual Bacteriorhodopsins. Science, 2000, 288, 143-146. (Pubitemid 30203048)
    • (2000) Science , vol.288 , Issue.5463 , pp. 143-146
    • Oesterhelt, F.1    Oesterhelt, D.2    Pfeiffer, M.3    Engel, A.4    Gaub, H.E.5    Muller, D.J.6
  • 22
    • 70350709999 scopus 로고    scopus 로고
    • Atomic force spectroscopy measures light activation and transducer binding induced structural changes in the sensory rhodopsin II
    • Oberbarnscheidt, L.; Janissen, R.; Martell, S.; Engelhard, M.; Oesterhelt, F. Atomic force spectroscopy measures light activation and transducer binding induced structural changes in the Sensory Rhodopsin II. J. Mol. Biol., 2009, 394(3), 383-390.
    • (2009) J. Mol. Biol. , vol.394 , Issue.3 , pp. 383-390
    • Oberbarnscheidt, L.1    Janissen, R.2    Martell, S.3    Engelhard, M.4    Oesterhelt, F.5
  • 23
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief, M.; Gautel, M;. Oesterhelt, F.; Fernandez, J.M.; Gaub, H.E. Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM. Science, 1997, 276, 1109-1112. (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 24
    • 0031021374 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model
    • DOI 10.1021/bi962014g
    • Haupts, U.; Tittor, J.; Bamberg, E.; Oesterhelt, D. General concept for ion translocation by halobacterial retinal proteins: the isomerization/ switch/transfer (IST) model. Biochemistry, 1997, 36(1), 2-7. (Pubitemid 27024671)
    • (1997) Biochemistry , vol.36 , Issue.1 , pp. 2-7
    • Haupts, U.1    Tittor, J.2    Bamberg, E.3    Oesterhelt, D.4
  • 25
    • 0342502772 scopus 로고
    • Functions of a new photoreceptor membrane
    • Oesterhelt, D.; Stoeckenius, W. Functions of a new photoreceptor membrane. Proc. Natl. Acad. Sci., 1973, 70(10), 2853-2857.
    • (1973) Proc. Natl. Acad. Sci. , vol.70 , Issue.10 , pp. 2853-2857
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 26
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin α-helices and loops analyzed by single-molecule force spectroscopy
    • Müller, D.J.; Kessler, M.; Oesterhelt, F.; Moller, C.; Oesterhelt, D.; Gaub, H. Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J., 2002, 83, 3578-3588. (Pubitemid 36041975)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3578-3588
    • Muller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 27
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • DOI 10.1006/jmbi.2001.4819
    • Bolen, D.W.; Baskakov, I.V. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol., 2001, 310, 955-963. (Pubitemid 32738368)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.5 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 29
    • 0026598013 scopus 로고
    • Enzyme stabilization be ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert, K.; Galinski, E.A. Enzyme stabilization be ectoine-type compatible solutes: protection against heating, freezing and drying. Appl. Microbiol. Biotechnol., 1992, 37, 61-65.
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 30
    • 33749031257 scopus 로고    scopus 로고
    • Extremolytes: Natural compounds from extremophiles for versatile applications
    • DOI 10.1007/s00253-006-0553-9
    • Lentzen, G.; Schwarz, T. Extremolytes: Natural compounds from extremophiles for versatile applications. Appl. Microbiol. Biotechnol., 2006, 72, 623-634. (Pubitemid 44454921)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.4 , pp. 623-634
    • Lentzen, G.1    Schwarz, T.2
  • 31
    • 77953689109 scopus 로고    scopus 로고
    • The effect of compatible solute ectoines on the structural organization of lipid monolayer and bilayer membranes
    • Harishchandra, R.K.; Wulff, S.; Lentzen, G.; Neuhaus, T.; Galla, H.J. The effect of compatible solute ectoines on the structural organization of lipid monolayer and bilayer membranes. Biophys. Chem., 2010, 150, 37-46.
    • (2010) Biophys. Chem. , vol.150 , pp. 37-46
    • Harishchandra, R.K.1    Wulff, S.2    Lentzen, G.3    Neuhaus, T.4    Galla, H.J.5
  • 32
    • 47649122833 scopus 로고    scopus 로고
    • Compatible solute influence on nucleic acids: Many questions but few answers
    • Kurz, M. Compatible solute influence on nucleic acids: many questions but few answers. Saline Systems, 2008, 4, 6.
    • (2008) Saline Systems , vol.4 , pp. 6
    • Kurz, M.1
  • 33
    • 34548552871 scopus 로고    scopus 로고
    • Microscopic understanding of preferential exclusion of compatible solute ectoine: Direct interaction and hydration alteration
    • DOI 10.1021/jp068367z
    • Yu, I.; Jindo, Y.; Nagaoka, M. Microscopic understanding of preferential exclusion of compatible solute ectoine: direct interaction and hydration alteration. J. Phys. Chem. B, 2007, 111, 10231-10238. (Pubitemid 47388029)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.34 , pp. 10231-10238
    • Yu, I.1    Jindo, Y.2    Nagaoka, M.3
  • 35
    • 77956022419 scopus 로고    scopus 로고
    • Enthalpically driven peptide stabilization by protective osmolytes
    • Politi, R.; Harries, D. Enthalpically driven peptide stabilization by protective osmolytes. Chem. Commun., 2010, 46, 6449-6451.
    • (2010) Chem. Commun. , vol.46 , pp. 6449-6451
    • Politi, R.1    Harries, D.2


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