메뉴 건너뛰기




Volumn 111, Issue 19, 2007, Pages 5344-5350

Interfacial water structure controls protein conformation

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; INTERFACES (MATERIALS); SALTS; SURFACE TENSION;

EID: 34249782027     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp066206p     Document Type: Article
Times cited : (85)

References (43)
  • 2
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins, K. D.; Washabaugh, M. W. The Hofmeister effect and the behaviour of water at interfaces. Q. Rev. Biophys. 1985, 18, 323-422.
    • (1985) Q. Rev. Biophys , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 5
    • 2142720593 scopus 로고    scopus 로고
    • Ion binding and ion specificity-the Hofmeister effect, Onsager and Lifschitz theories
    • Ninham, B. W.; Yaminsky, V. V. Ion binding and ion specificity-the Hofmeister effect, Onsager and Lifschitz theories. Langmuir 1997, 13, 2097-2108.
    • (1997) Langmuir , vol.13 , pp. 2097-2108
    • Ninham, B.W.1    Yaminsky, V.V.2
  • 6
    • 0037031425 scopus 로고    scopus 로고
    • Ion specificity of micelles and and microemulsions explained by ionic dispersion forces
    • Bostrom, M.; Williams, D. R.; Ninham, B. W. Ion specificity of micelles and and microemulsions explained by ionic dispersion forces. Langmuir 2002, 18, 6010-6014.
    • (2002) Langmuir , vol.18 , pp. 6010-6014
    • Bostrom, M.1    Williams, D.R.2    Ninham, B.W.3
  • 8
    • 0003516749 scopus 로고
    • Oxford University Press: Oxford, U.K
    • Atkins, P. W. Physical Chemistry; Oxford University Press: Oxford, U.K., 1990.
    • (1990) Physical Chemistry
    • Atkins, P.W.1
  • 10
    • 0000804935 scopus 로고
    • Ueber die Konstitution der Salzlösungen auf Grund ihres Verhaltens zu Kohlensäure
    • Setschenow, J. Ueber die Konstitution der Salzlösungen auf Grund ihres Verhaltens zu Kohlensäure. Z. Phys. Chem. 1889, 4, 117-125.
    • (1889) Z. Phys. Chem , vol.4 , pp. 117-125
    • Setschenow, J.1
  • 11
    • 0001133638 scopus 로고
    • Concerning the physical characteristics of solutions in correlation II. Surface tension and electronic conductivity of watery salt solutions
    • Heydweiller, A. Concerning the physical characteristics of solutions in correlation II. Surface tension and electronic conductivity of watery salt solutions. Ann. Phys. 1910, 33, 145-185.
    • (1910) Ann. Phys , vol.33 , pp. 145-185
    • Heydweiller, A.1
  • 12
    • 0017623134 scopus 로고
    • Salt effects on hydrophobic interactions in precipitation and chromatography of proteins
    • Melander, W.; Horváth, Cs. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins. Arch. Biochem. Biophys. 1977, 183, 200-215.
    • (1977) Arch. Biochem. Biophys , vol.183 , pp. 200-215
    • Melander, W.1    Horváth, C.2
  • 13
    • 0029792830 scopus 로고    scopus 로고
    • Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. How Hofmeister ion interactions affect protein stability. Biophys. J. 1996, 71, 2056-2063.
    • (1996) Biophys. J , vol.71 , pp. 2056-2063
    • Baldwin, R.1    How, L.2
  • 14
    • 0020477047 scopus 로고
    • Preferential ineraction of proteins with salts in concentrated solutions
    • Arakawa, T.; Timasheff, S. N. Preferential ineraction of proteins with salts in concentrated solutions. Biochemistry 1982, 21, 6545-6552.
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 15
    • 36549093231 scopus 로고
    • Effect of salts on dynamics of water: A Raman spectroscopic study
    • Terpstra, P.: Combes, D.; Zwick, A. Effect of salts on dynamics of water: A Raman spectroscopic study. J. Chem. Phys. 1990, 99, 65-70.
    • (1990) J. Chem. Phys , vol.99 , pp. 65-70
    • Terpstra, P.1    Combes, D.2    Zwick, A.3
  • 16
    • 0002619244 scopus 로고
    • Effect of high salt concentrations on water structure
    • Leberman, R.; Soper, A. K. Effect of high salt concentrations on water structure. Nature 1995, 378, 364-366.
    • (1995) Nature , vol.378 , pp. 364-366
    • Leberman, R.1    Soper, A.K.2
  • 17
    • 10944236508 scopus 로고    scopus 로고
    • Temperature dependence of water vibrational spectrum: A molecular dynamics simulation study
    • Praprotnik, M.: Janezic, D.; Mavri, J. Temperature dependence of water vibrational spectrum: a molecular dynamics simulation study. J. Phys. Chem. A 2004, 108, 11056-11062.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 11056-11062
    • Praprotnik, M.1    Janezic, D.2    Mavri, J.3
  • 18
    • 0038115064 scopus 로고    scopus 로고
    • Negligible effect of ions on the hydrogen-bond structure in liquid water
    • Omta, A. W.; Kropman, M. F.; Woutersen, S.; Bakker, H. J. Negligible effect of ions on the hydrogen-bond structure in liquid water. Science 2003, 301, 347-349.
    • (2003) Science , vol.301 , pp. 347-349
    • Omta, A.W.1    Kropman, M.F.2    Woutersen, S.3    Bakker, H.J.4
  • 19
    • 0042973013 scopus 로고    scopus 로고
    • Specific ion effects via ion hydration: I. Surface tension
    • Manciu, M.; Ruckenstein, E. Specific ion effects via ion hydration: I. Surface tension. Adv. Colloid Interface Sci. 2003, 105, 63-101.
    • (2003) Adv. Colloid Interface Sci , vol.105 , pp. 63-101
    • Manciu, M.1    Ruckenstein, E.2
  • 20
    • 33846080680 scopus 로고
    • Surface potentials of aqueous electrolyte solutions
    • Jarvis N. L. Surface potentials of aqueous electrolyte solutions. J. Phys. Chem. 1968, 72, 74-79.
    • (1968) J. Phys. Chem , vol.72 , pp. 74-79
    • Jarvis, N.L.1
  • 21
    • 0030040794 scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • Lin, T.-Y.; Timasheff, S. N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 1995, 5, 372-381.
    • (1995) Protein Sci , vol.5 , pp. 372-381
    • Lin, T.-Y.1    Timasheff, S.N.2
  • 22
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: A balance of contact interaction and excluded volume
    • Schellman, J. A. Protein stability in mixed solvents: A balance of contact interaction and excluded volume. Biophys. J. 2003, 85, 108-125.
    • (2003) Biophys. J , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 23
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B.; Richards, F. M. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 1971, 55, 379-400.
    • (1971) J. Mol. Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 24
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • Chothia, C. Hydrophobic bonding and accessible surface area in proteins. Nature 1974, 248, 338-339.
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1
  • 25
    • 0018318966 scopus 로고
    • Interfacial free energy and the hydrophobic effect
    • Tanford, C. Interfacial free energy and the hydrophobic effect. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 4175-4176.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 4175-4176
    • Tanford, C.1
  • 26
    • 0026416668 scopus 로고
    • Reconciling the magnitude of microscopic and macroscopic hydrophobic effects
    • Sharp, K. A.; Nicholls, A.; Fine, R. F.; Honig, B. Reconciling the magnitude of microscopic and macroscopic hydrophobic effects. Science 1991, 252, 106-109.
    • (1991) Science , vol.252 , pp. 106-109
    • Sharp, K.A.1    Nicholls, A.2    Fine, R.F.3    Honig, B.4
  • 27
    • 0001764065 scopus 로고
    • Microscopic surface tension down to molecular dimensions and microthermodynamic surface areas of molecules or clusters
    • Sinanoglu, O. Microscopic surface tension down to molecular dimensions and microthermodynamic surface areas of molecules or clusters. J. Chem. Phys. 1981, 75, 463-468.
    • (1981) J. Chem. Phys , vol.75 , pp. 463-468
    • Sinanoglu, O.1
  • 28
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler, D. Interfaces and the driving force of hydrophobic assembly. Nature 2005, 437, 640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 29
    • 36149028105 scopus 로고
    • Irreversibility and generalized noise
    • Callen, H. B.; Weiten, T. A. Irreversibility and generalized noise. Phys. Rev. 1951, 83, 34-40.
    • (1951) Phys. Rev , vol.83 , pp. 34-40
    • Callen, H.B.1    Weiten, T.A.2
  • 30
    • 0004043557 scopus 로고
    • Welch, E. R, Ed, Wiley: New York
    • Welch, E. R., Ed. The Fluctuating Enzyme; Wiley: New York, 1986.
    • (1986) The Fluctuating Enzyme
  • 31
    • 0031856943 scopus 로고    scopus 로고
    • Evidence for loosening of a protein mechanism
    • Dér, A.; Ramsden, J. J. Evidence for loosening of a protein mechanism. Naturwissenschaften 1998, 85, 353-355.
    • (1998) Naturwissenschaften , vol.85 , pp. 353-355
    • Dér, A.1    Ramsden, J.J.2
  • 32
    • 0034865767 scopus 로고    scopus 로고
    • Fluctuations and the Hofmeister effect
    • Neagu, A.; Neagu, M.; Dér, A. Fluctuations and the Hofmeister effect. Biophys. J. 2001, 81, 1285-1294.
    • (2001) Biophys. J , vol.81 , pp. 1285-1294
    • Neagu, A.1    Neagu, M.2    Dér, A.3
  • 34
  • 36
    • 0018789853 scopus 로고
    • Bacteriorhodopsin and the purple membrane of Halobacteria
    • Stoeckenius, W.; Lozier, R. H.; and Bogomolni, R. Bacteriorhodopsin and the purple membrane of Halobacteria. Biochim. Biophys. Acta 1979, 505, 215-278.
    • (1979) Biochim. Biophys. Acta , vol.505 , pp. 215-278
    • Stoeckenius, W.1    Lozier, R.H.2    Bogomolni, R.3
  • 37
    • 0020489247 scopus 로고
    • Infrared spectrum of purple membraneclue to a proton conduction mechanism
    • Krimm, S.; Dwivedi, A. M. Infrared spectrum of purple membraneclue to a proton conduction mechanism. Science 1982, 216, 407-408.
    • (1982) Science , vol.216 , pp. 407-408
    • Krimm, S.1    Dwivedi, A.M.2
  • 38
    • 0034033871 scopus 로고    scopus 로고
    • The effect of protein conformational change from alpha(II) to alpha(I) on the bacteriorhodopsin photocycle
    • Wang, J.; El-Sayed, M. The effect of protein conformational change from alpha(II) to alpha(I) on the bacteriorhodopsin photocycle. Biophys. J. 2000, 78, 2031-2036.
    • (2000) Biophys. J , vol.78 , pp. 2031-2036
    • Wang, J.1    El-Sayed, M.2
  • 39
    • 4043104885 scopus 로고    scopus 로고
    • Pressure-induced transmembrane alpha(II) to alpha(I) helical conversion in bacteriorhodopsin: An infrared spectroscopic study
    • Barnett, S. M.; Edwards, C. M.; Butler, I. S.; Levin, I. W. Pressure-induced transmembrane alpha(II) to alpha(I) helical conversion in bacteriorhodopsin: An infrared spectroscopic study. J. Phys. Chem. B 1997, 101, 9421-9424.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 9421-9424
    • Barnett, S.M.1    Edwards, C.M.2    Butler, I.S.3    Levin, I.W.4
  • 40
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D.; Stoeckenius, W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 1974, 31, 667-678.
    • (1974) Methods Enzymol , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 41
    • 0029032977 scopus 로고
    • A pathway for the thermal destabilization of bacteriorhodopsin
    • Taneva, S. G.; Caaveiro, J. M. M.; Muga, A.; Goni, F. M. A pathway for the thermal destabilization of bacteriorhodopsin. FEBS Lett. 1995, 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
  • 43
    • 34249814796 scopus 로고    scopus 로고
    • Active transport modulated by barrier fluctuations
    • Dér, A, Keszthelyi, L, Eds, IOS Press: Amsterdam, The Netherlands
    • Neagu, A.; Neagu, M.; Dér, A. Active transport modulated by barrier fluctuations. In Bioelectronic Applications of Photochromic Pigments; Dér, A., Keszthelyi, L., Eds.; IOS Press: Amsterdam, The Netherlands, 2001.
    • (2001) Bioelectronic Applications of Photochromic Pigments
    • Neagu, A.1    Neagu, M.2    Dér, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.