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Volumn 135, Issue 17, 2011, Pages

Hydrophobic interactions in presence of osmolytes urea and trimethylamine-N-oxide

Author keywords

[No Author keywords available]

Indexed keywords

HYDRATION SHELL; HYDROPHOBIC INTERACTIONS; HYDROPHOBIC MOIETIES; LIFE-TIMES; MOLECULAR DYNAMICS SIMULATIONS; NATURALLY OCCURRING; NEOPENTANE; ORIENTATIONAL DISTRIBUTIONS; OSMOLYTES; OVER WATER; PREFERENTIAL SOLVATION; PURE WATER; WATER LAYERS; WATER MOLECULE; WATER STRUCTURE; WATER-WATER;

EID: 80855156841     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3655672     Document Type: Article
Times cited : (41)

References (66)
  • 2
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • DOI 10.1038/nature04162, PII N04162
    • D. Chandler, Nature (London) 437, 640 (2005), and references therein. 10.1038/nature04162 (Pubitemid 41486526)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 640-647
    • Chandler, D.1
  • 4
    • 0030912208 scopus 로고    scopus 로고
    • references therein. 10.1002/pro.5560060627
    • C. Tanford, Protein Sci. 6, 1358 (1997), and references therein. 10.1002/pro.5560060627
    • (1997) Protein Sci. , vol.6 , pp. 1358
    • Tanford, C.1
  • 5
    • 33646904758 scopus 로고    scopus 로고
    • Protein folding-simulation
    • DOI 10.1021/cr0404242
    • V. Daggett, Chem. Rev. 106, 1898 (2006), and references therein. 10.1021/cr0404242 (Pubitemid 43792785)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1898-1916
    • Daggett, V.1
  • 7
    • 23244452958 scopus 로고    scopus 로고
    • Effect of urea on peptide conformation in water: Molecular dynamics and experimental characterization
    • DOI 10.1529/biophysj.105.061978
    • A. Caballero-Herrera, K. Nordstrand, K. D. Berndt, and L. Nilsson, Biophys. J. 89, 842 (2005). 10.1529/biophysj.105.061978 (Pubitemid 41098971)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 842-857
    • Caballero-Herrera, A.1    Nordstrand, K.2    Berndt, K.D.3    Nilsson, L.4
  • 8
    • 0037442337 scopus 로고    scopus 로고
    • Molecular dynamics simulations of end-to-end contact formation in hydrocarbon chains in water and aqueous urea solution
    • DOI 10.1021/ja020496f
    • R. D. Mountain and D. Thirumalai, J. Am. Chem. Soc. 125, 1950 (2003). 10.1021/ja020496f (Pubitemid 36232587)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1950-1957
    • Mountain, R.D.1    Thirumalai, D.2
  • 10
    • 46449109015 scopus 로고    scopus 로고
    • 10.1146/annurev.biochem.77.061306.131357
    • D. W. Bolen and G. D. Rose, Annu. Rev. Biochem. 77, 339 (2008). 10.1146/annurev.biochem.77.061306.131357
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 339
    • Bolen, D.W.1    Rose, G.D.2
  • 13
    • 20444474170 scopus 로고    scopus 로고
    • A natural osmolyte trimethylamine N-oxide promotes assembly and bundling of the bacterial cell division protein, FtsZ and counteracts the denaturing effects of urea
    • DOI 10.1111/j.1742-4658.2005.04696.x
    • A. Mukherjee, M. K. Santra, T. K. Beuria, and D. Panda, FEBS J. 272, 2760 (2005). 10.1111/j.1742-4658.2005.04696.x (Pubitemid 40825423)
    • (2005) FEBS Journal , vol.272 , Issue.11 , pp. 2760-2772
    • Mukherjee, A.1    Santra, M.K.2    Beuria, T.K.3    Panda, D.4
  • 14
    • 33947488954 scopus 로고
    • 10.1021/ja01064a028
    • C. Tanford, J. Am. Chem. Soc. 86, 2050 (1964). 10.1021/ja01064a028
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 2050
    • Tanford, C.1
  • 16
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • DOI 10.1021/bi970247h
    • A. Wang, and D. W. Bolen, Biochemistry 36, 9101 (1997). 10.1021/bi970247h (Pubitemid 27329494)
    • (1997) Biochemistry , vol.36 , Issue.30 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 17
    • 0028862864 scopus 로고
    • 10.1021/bi00039a051
    • Y. Liu, and D. W. Bolen, Biochemistry 34, 12884 (1995). 10.1021/bi00039a051
    • (1995) Biochemistry , vol.34 , pp. 12884
    • Liu, Y.1    Bolen, D.W.2
  • 18
    • 0032570873 scopus 로고    scopus 로고
    • Forcing thermodynamically unfolded proteins to fold
    • DOI 10.1074/jbc.273.9.4831
    • I. Baskakov, and D. W. Bolen, J. Biol. Chem. 273, 4831 (1998). 10.1074/jbc.273.9.4831 (Pubitemid 28108630)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.9 , pp. 4831-4834
    • Baskakov, I.1    Bolen, D.W.2
  • 19
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • DOI 10.1006/jmbi.2001.4819
    • D. W. Bolen, and I. Baskakov, J. Mol. Biol. 310, 955 (2001). 10.1006/jmbi.2001.4819 (Pubitemid 32738368)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.5 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 27
    • 23244459863 scopus 로고    scopus 로고
    • Osmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: Origin of osmolyte compatibility
    • DOI 10.1529/biophysj.104.056671
    • M. V. Athawale, J. S. Dordick, and S. Garde, Biophys. J. 89, 858 (2005). 10.1529/biophysj.104.056671 (Pubitemid 41098972)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 858-866
    • Athawale, M.V.1    Dordick, J.S.2    Garde, S.3
  • 28
    • 34547534081 scopus 로고    scopus 로고
    • The influence of urea and trimethylamine-N-oxide on hydrophobic interactions
    • DOI 10.1021/jp0733668
    • S. Paul and G. N. Patey, J. Phys. Chem. B 111, 7932 (2007). 10.1021/jp0733668 (Pubitemid 47184362)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.28 , pp. 7932-7933
    • Paul, S.1    Patey, G.N.2
  • 29
    • 34247121912 scopus 로고    scopus 로고
    • Structure and interaction in aqueous urea - Trimethylamine-N-oxide solutions
    • DOI 10.1021/ja0685506
    • S. Paul and G. N. Patey, J. Am. Chem. Soc. 129, 4476 (2007). 10.1021/ja0685506 (Pubitemid 46595464)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.14 , pp. 4476-4482
    • Paul, S.1    Patey, G.N.2
  • 45
    • 34249806047 scopus 로고    scopus 로고
    • Preferential solvation in urea solutions at different concentrations: Properties from simulation studies
    • DOI 10.1021/jp067659x
    • H. Kokubo and B. M. Pettitt, J. Phys. Chem. B 111, 5233 (2007). 10.1021/jp067659x (Pubitemid 46854511)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.19 , pp. 5233-5242
    • Kokubo, H.1    Pettitt, B.M.2
  • 46
    • 0013096029 scopus 로고
    • 10.1021/j100346a086
    • A. Ben-Naim, J. Phys. Chem. 93, 3809 (1989). 10.1021/j100346a086
    • (1989) J. Phys. Chem. , vol.93 , pp. 3809
    • Ben-Naim, A.1
  • 53
    • 0141560450 scopus 로고    scopus 로고
    • Impact of urea on water structure: A clue to its properties as a denaturant?
    • DOI 10.1016/S0301-4622(03)00095-4
    • A. K. Soper, E. W. Castner, and A. Luzar, Biophys. Chem. 105, 649 (2003). 10.1016/S0301-4622(03)00095-4 (Pubitemid 37123089)
    • (2003) Biophysical Chemistry , vol.105 , Issue.2-3 , pp. 649-666
    • Soper, A.K.1    Castner, E.W.2    Luzar, A.3
  • 55
    • 27644444686 scopus 로고    scopus 로고
    • Liquid-vapor interfaces of water-acetonitrile mixtures of varying composition
    • DOI 10.1063/1.2102892, 184706
    • S. Paul and A. Chandra, J. Chem. Phys. 123, 184706 (2005). 10.1063/1.2102892 (Pubitemid 41580123)
    • (2005) Journal of Chemical Physics , vol.123 , Issue.18 , pp. 1-8
    • Paul, S.1    Chandra, A.2
  • 59
  • 60
    • 0034504583 scopus 로고    scopus 로고
    • Resolving the hydrogen bond dynamics conundrum
    • DOI 10.1063/1.1320826
    • A. Luzar, J. Chem. Phys. 113, 10663 (2000). 10.1063/1.1320826 (Pubitemid 32076963)
    • (2000) Journal of Chemical Physics , vol.113 , Issue.23 , pp. 10663-10675
    • Luzar, A.1
  • 61
    • 4243838224 scopus 로고    scopus 로고
    • 10.1103/PhysRevLett.85.768
    • A. Chandra, Phys. Rev. Lett. 85, 768 (2000); 10.1103/PhysRevLett.85.768
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 768
    • Chandra, A.1
  • 62
    • 0038270185 scopus 로고    scopus 로고
    • 10.1021/jp022147d
    • A. Chandra, J. Phys. Chem. B 107, 3899 (2003). 10.1021/jp022147d
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3899
    • Chandra, A.1
  • 64
    • 1442312012 scopus 로고    scopus 로고
    • 10.1016/j.cplett.2003.12.120
    • S. Paul and A. Chandra, Chem. Phys. Lett. 386, 218 (2004); 10.1016/j.cplett.2003.12.120
    • (2004) Chem. Phys. Lett. , vol.386 , pp. 218
    • Paul, S.1    Chandra, A.2
  • 66
    • 0000866097 scopus 로고
    • 10.1080/00268978300102931
    • D. Rapaport, Mol. Phys. 50, 1151 (1983). 10.1080/00268978300102931
    • (1983) Mol. Phys. , vol.50 , pp. 1151
    • Rapaport, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.