메뉴 건너뛰기




Volumn 184, Issue , 2013, Pages 8-16

Protonation of trimethylamine N-oxide (TMAO) is required for stabilization of RNA tertiary structure

Author keywords

Constant pH simulations; Molecular dynamics simulations; RNA folding; RNA tertiary structure

Indexed keywords

HYDROGEN; PHOSPHATE; QUEUOSINE; RNA; TRIMETHYLAMINE OXIDE;

EID: 84883281341     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.08.002     Document Type: Article
Times cited : (25)

References (35)
  • 1
    • 35448999589 scopus 로고    scopus 로고
    • A practical guide on how osmolytes modulate macromolecular properties
    • D. Harries, and J. Rosgen A practical guide on how osmolytes modulate macromolecular properties Methods Cell Biol. 84 2008 679 735
    • (2008) Methods Cell Biol. , vol.84 , pp. 679-735
    • Harries, D.1    Rosgen, J.2
  • 2
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • P.H. Yancey, M.E. Clark, S.C. Hand, R.D. Bowlus, and G.N. Somero Living with water stress: evolution of osmolyte systems Science 217 1982 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
  • 4
    • 23044529588 scopus 로고    scopus 로고
    • Water stress, osmolytes and proteins
    • P.H. Yancey Water stress, osmolytes and proteins Am. Zool. 41 2001 699 709 (Pubitemid 33770242)
    • (2001) American Zoologist , vol.41 , Issue.4 , pp. 699-709
    • Yancey, P.H.1
  • 5
    • 51649087154 scopus 로고    scopus 로고
    • Effects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model
    • E.P. O'Brien, G. Ziv, G. Haran, B.R. Brooks, and D. Thirumalai Effects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model Proc. Natl. Acad. Sci. U. S. A. 105 2008 13403 13408
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13403-13408
    • O'Brien, E.P.1    Ziv, G.2    Haran, G.3    Brooks, B.R.4    Thirumalai, D.5
  • 7
    • 0037138672 scopus 로고    scopus 로고
    • The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea
    • DOI 10.1021/ja004206b
    • Q. Zou, B.J. Bennion, V. Daggett, and K.P. Murphy The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea J. Am. Chem. Soc. 124 2002 1192 1202 (Pubitemid 34169126)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.7 , pp. 1192-1202
    • Zou, Q.1    Bennion, B.J.2    Daggett, V.3    Murphy, K.P.4
  • 8
    • 0037448912 scopus 로고    scopus 로고
    • Trimethylamine N-oxide stabilizes RNA tertiary structure and attenuates the denaturating effects of urea
    • DOI 10.1021/ja0292997
    • T.C. Gluick, and S. Yadav Trimethylamine N-oxide stabilizes RNA tertiary structure and attenuates the denaturating effects of urea J. Am. Chem. Soc. 125 2003 4418 4419 (Pubitemid 36418678)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.15 , pp. 4418-4419
    • Gluick, T.C.1    Yadav, S.2
  • 10
    • 44949181944 scopus 로고    scopus 로고
    • Effects of trimethylamine N-Oxide (TMAO) and crowding agents on the stability of RNA hairpins
    • DOI 10.1021/ja078326w
    • D. Pincus, C. Hyeon, and D. Thirumalai Effects of trimethylamine N-oxide (TMAO) and crowding agents on the stability of RNA hairpins J. Am. Chem. Soc. 130 2008 7364 7372 (Pubitemid 351813229)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.23 , pp. 7364-7372
    • Pincus, D.L.1    Hyeon, C.2    Thirumalai, D.3
  • 11
    • 78049445847 scopus 로고    scopus 로고
    • 2+: Evidence for a large barrier to folding from phosphate dehydration
    • 2+: evidence for a large barrier to folding from phosphate dehydration J. Mol. Biol. 404 2010 138 157
    • (2010) J. Mol. Biol. , vol.404 , pp. 138-157
    • Lambert, D.1    Leipply, D.2    Draper, D.E.3
  • 13
    • 23244440384 scopus 로고    scopus 로고
    • Constant pH molecular dynamics with proton tautomerism
    • DOI 10.1529/biophysj.105.061341
    • J. Khandogin, and C.L. Brooks Constant pH molecular dynamics with proton tautomerism Biophys. J. 89 2005 141 157 (Pubitemid 41098271)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 141-157
    • Khandogin, J.1    Brooks III, C.L.2
  • 15
    • 79955484353 scopus 로고    scopus 로고
    • Impact of 2′-hydroxyl sampling on the conformational properties of RNA: Update of the CHARMM all-atom additive force field for RNA
    • E.J. Denning, U.D. Priyakumar, L. Nilsson, and A.D. MacKerell Jr. Impact of 2′-hydroxyl sampling on the conformational properties of RNA: update of the CHARMM all-atom additive force field for RNA J. Comp. Chem. 32 2011 1929 1943
    • (2011) J. Comp. Chem. , vol.32 , pp. 1929-1943
    • Denning, E.J.1    Priyakumar, U.D.2    Nilsson, L.3    Mackerell, Jr.A.D.4
  • 16
    • 0033104039 scopus 로고    scopus 로고
    • New tricks for modelers from the crystallography toolkit: The particle mesh Ewald algorithm and its use in nucleic acid simulations
    • T. Darden, L. Perera, L. Li, and L. Pedersen New tricks for modelers from the crystallography toolkit: the particle mesh Ewald algorithm and its use in nucleic acid simulations Structure 7 1999 R55 R60
    • (1999) Structure , vol.7
    • Darden, T.1    Perera, L.2    Li, L.3    Pedersen, L.4
  • 17
    • 0000951252 scopus 로고    scopus 로고
    • Effect of electrostatic force truncation on interfacial and transport properties of water
    • S.E. Feller, R.W. Pastor, A. Rojnuckarin, S. Bogusz, and B.R. Brooks Effect of electrostatic force truncation on interfacial and transport properties of water J. Phys. Chem. 100 1996 17011 17020 (Pubitemid 126787137)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.42 , pp. 17011-17020
    • Feller, S.E.1    Pastor, R.W.2    Rojnuckarin, A.3    Bogusz, S.4    Brooks, B.R.5
  • 18
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • S.E. Feller, Y. Zhang, R.W. Pastor, and B.R. Brooks Constant pressure molecular dynamics simulation: the Langevin piston method J. Chem. Phys. 103 1995 4613 4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 19
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular-dynamics methods
    • S. Nose A unified formulation of the constant temperature molecular-dynamics methods J. Chem. Phys. 81 1984 511 519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nose, S.1
  • 20
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 21
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkane
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkane J. Comp. Phys. 23 1977 327 341
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 24
    • 77953905304 scopus 로고    scopus 로고
    • a Values with continuous constant pH molecular dynamics
    • a Values with continuous constant pH molecular dynamics Biothermodynamics, Part A 466 2009 455 475
    • (2009) Biothermodynamics, Part A , vol.466 , pp. 455-475
    • Wallace, J.A.1    Shen, J.K.2
  • 25
    • 0141956090 scopus 로고    scopus 로고
    • Generalized Born model with a simple smoothing function
    • W. Im, M.S. Lee, and C.L. Brooks Generalized Born model with a simple smoothing function J. Comput. Chem. 24 2003 1691 1702
    • (2003) J. Comput. Chem. , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2    Brooks, C.L.3
  • 26
    • 79958185452 scopus 로고    scopus 로고
    • MDAnalysis: A toolkit for the analysis of molecular dynamics simulations
    • N. Michaud-Agrawal, E.J. Denning, T.B. Woolf, and O. Beckstein MDAnalysis: a toolkit for the analysis of molecular dynamics simulations J. Comput. Chem. 32 2011 2319 2327
    • (2011) J. Comput. Chem. , vol.32 , pp. 2319-2327
    • Michaud-Agrawal, N.1    Denning, E.J.2    Woolf, T.B.3    Beckstein, O.4
  • 27
  • 28
    • 0028150954 scopus 로고
    • Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein
    • DOI 10.1021/bi00208a021
    • T.Y. Lin, and S.N. Timasheff Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein Biochemistry 33 1994 12695 12701 (Pubitemid 24345902)
    • (1994) Biochemistry , vol.33 , Issue.42 , pp. 12695-12701
    • Lin, T.-Y.1    Timasheff, S.N.2
  • 29
    • 0038290339 scopus 로고    scopus 로고
    • Hydrogen exchange kinetics of RNase A and the urea: TMAO paradigm
    • DOI 10.1021/bi0206457
    • Q. Youxing, and D.W. Bolen Hydrogen exchange kinetics of RNase A and the urea:TMAO paradigm Biochemistry 42 2003 5837 5849 (Pubitemid 36582876)
    • (2003) Biochemistry , vol.42 , Issue.19 , pp. 5837-5849
    • Qu, Y.1    Bolen, D.W.2
  • 30
    • 15744404427 scopus 로고    scopus 로고
    • a: Measurements of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide
    • DOI 10.1074/jbc.M410716200
    • a measurements of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide J. Biol. Chem. 280 2005 11035 11042 (Pubitemid 40418406)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11035-11042
    • Singh, R.1    Haque, I.2    Ahmad, F.3
  • 31
    • 84868091323 scopus 로고    scopus 로고
    • Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape
    • A.C.M. Ferreon, M.M. Moosa, G. Yann, and A.A. Deniz Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape Proc. Natl. Acad. Sci. U. S. A. 109 2012 17770 17771
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 17770-17771
    • Ferreon, A.C.M.1    Moosa, M.M.2    Yann, G.3    Deniz, A.A.4
  • 32
    • 84855710487 scopus 로고    scopus 로고
    • Constant pH molecular dynamics simulations of nucleic acids in explicit solvent
    • G. Goh, J. Knight, and C.I. Brooks Constant pH molecular dynamics simulations of nucleic acids in explicit solvent J. Chem. Theory Comput. 8 2012 36 46
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 36-46
    • Goh, G.1    Knight, J.2    Brooks, C.I.3
  • 33
    • 84873645505 scopus 로고    scopus 로고
    • PH-dependent dynamics of complex RNA macromolecules
    • G. Goh, J. Knight, and C.L. Brooks pH-dependent dynamics of complex RNA macromolecules J. Chem. Theory Comput. 9 2013 935 943
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 935-943
    • Goh, G.1    Knight, J.2    Brooks, C.L.3
  • 34
    • 77749286433 scopus 로고    scopus 로고
    • 2+ concentration: Interpretation of the Hill equation and coefficient
    • 2+ concentration: interpretation of the Hill equation and coefficient Biochemistry 49 2010 1843 1853
    • (2010) Biochemistry , vol.49 , pp. 1843-1853
    • Leipply, D.1    Draper, D.E.2
  • 35
    • 0035830964 scopus 로고    scopus 로고
    • Role of counterion condensation in folding of the Tetrahymena ribozyme. I. Equilibrium stabilization by cations
    • DOI 10.1006/jmbi.2001.4437
    • S. Heilman-Miller, D. Thirumalai, and S.A. Woodson Role of counterion condensation in folding of the Tetrahymena ribozyme. I. Equilibrium stabilization by cations J. Mol. Biol. 306 2001 1157 1166 (Pubitemid 33030011)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.5 , pp. 1157-1166
    • Heilman-Miller, S.L.1    Thirumalai, D.2    Woodson, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.