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Volumn 95, Issue 7, 2008, Pages 3391-3399

Potential for modulation of the hydrophobic effect inside chaperonins

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; NANOMATERIAL; SOLVENT; WATER;

EID: 55949101455     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.131037     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70:603-647.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 2
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 4
    • 0344738987 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: Fate of substrate polypeptide
    • Fenton, W. A., and A. L. Horwich. 2003. Chaperonin-mediated protein folding: fate of substrate polypeptide. Q. Rev. Biophys. 36:229-256.
    • (2003) Q. Rev. Biophys , vol.36 , pp. 229-256
    • Fenton, W.A.1    Horwich, A.L.2
  • 5
    • 0035913902 scopus 로고    scopus 로고
    • Dual function of protein confinement in chaperonin-assisted protein folding
    • Brinker, A., G. Pfeifer, M. J. Kerner, D. J. Naylor, F. U. Hartl, and M. Hayer-Hartl. 2001. Dual function of protein confinement in chaperonin-assisted protein folding. Cell. 107:223-233.
    • (2001) Cell , vol.107 , pp. 223-233
    • Brinker, A.1    Pfeifer, G.2    Kerner, M.J.3    Naylor, D.J.4    Hartl, F.U.5    Hayer-Hartl, M.6
  • 7
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler, D. 2005. Interfaces and the driving force of hydrophobic assembly. Nature. 437:640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 8
    • 0000866128 scopus 로고
    • Hydrophobic effect in protein folding and other noncovalent processes involving proteins
    • Spolar, R., J. Ha, and M. Record. 1989. Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc. Natl. Acad. Sci. USA. 86:8382-8385.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8382-8385
    • Spolar, R.1    Ha, J.2    Record, M.3
  • 9
    • 0035817917 scopus 로고    scopus 로고
    • Fluidity of water confined to subnanometre films
    • Raviv, U., P. Laurat, and J. Klein. 2001. Fluidity of water confined to subnanometre films. Nature. 413:51-54.
    • (2001) Nature , vol.413 , pp. 51-54
    • Raviv, U.1    Laurat, P.2    Klein, J.3
  • 10
    • 33746685028 scopus 로고    scopus 로고
    • Super-hydrophobicity: Drying transition of confined water
    • Singh, S., J. Houston, F. v. Swol, and C. J. Brinker. 2006. Super-hydrophobicity: drying transition of confined water. Nature. 442:526.
    • (2006) Nature , vol.442 , pp. 526
    • Singh, S.1    Houston, J.2    Swol, F.V.3    Brinker, C.J.4
  • 11
    • 33748764682 scopus 로고    scopus 로고
    • Unusual hydrogen bonding in water-filled carbon nanotubes
    • Byl, O., J. Liu, Y. Wang, W. Yim, J. K. Johnson, and J. T. Yates. 2006. Unusual hydrogen bonding in water-filled carbon nanotubes. J. Am. Chem. Soc. 128:12090-12097.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 12090-12097
    • Byl, O.1    Liu, J.2    Wang, Y.3    Yim, W.4    Johnson, J.K.5    Yates, J.T.6
  • 12
    • 0035850349 scopus 로고    scopus 로고
    • Salting-in and salting-out of hydrophobic solutes in aqueous salt solutions
    • Kalra, A., N. Tugcu, S. M. Cramer, and S. Garde. 2001. Salting-in and salting-out of hydrophobic solutes in aqueous salt solutions. J. Phys. Chem. B. 105:6380-6386.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6380-6386
    • Kalra, A.1    Tugcu, N.2    Cramer, S.M.3    Garde, S.4
  • 13
    • 12344271184 scopus 로고    scopus 로고
    • On the salt-induced stabilization of pair and many-body hydrophobic interactions
    • Ghosh, T., A. Kalra, and S. Garde. 2005. On the salt-induced stabilization of pair and many-body hydrophobic interactions. J. Phys. Chem. B. 109:642-651.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 642-651
    • Ghosh, T.1    Kalra, A.2    Garde, S.3
  • 14
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: Salt and solvent effects on interfacial phenomena
    • Cacace, M. G., E. M. Landau, and J. J. Ramsden. 1997. The Hofmeister series: salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 30:241-277.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 17
    • 0347319435 scopus 로고    scopus 로고
    • Reduction of the hydrophobic attraction between charged solutes in water
    • Dzubiella, J., and J.-P. Hansen. 2003. Reduction of the hydrophobic attraction between charged solutes in water. J. Chem. Phys. 119:12049-12052.
    • (2003) J. Chem. Phys , vol.119 , pp. 12049-12052
    • Dzubiella, J.1    Hansen, J.-P.2
  • 18
    • 4944246231 scopus 로고    scopus 로고
    • Competition of hydrophobic and Coulombic interactions between nanosized solutes
    • Dzubiella, J., and J.-P. Hansen. 2004. Competition of hydrophobic and Coulombic interactions between nanosized solutes. J. Chem. Phys. 121:5514-5530.
    • (2004) J. Chem. Phys , vol.121 , pp. 5514-5530
    • Dzubiella, J.1    Hansen, J.-P.2
  • 19
    • 33750077790 scopus 로고    scopus 로고
    • Hydrophobic and ionic interactions in nanosized water droplets
    • Vaitheeswaran, S., and D. Thirumalai. 2006. Hydrophobic and ionic interactions in nanosized water droplets. J. Am. Chem. Soc. 128:13490-13496.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 13490-13496
    • Vaitheeswaran, S.1    Thirumalai, D.2
  • 20
    • 22144481993 scopus 로고    scopus 로고
    • Hydrophobic hydration from small to large lengthscales: Understanding and manipulating the crossover
    • Rajamani, S., T. Truskett, and S. Garde. 2005. Hydrophobic hydration from small to large lengthscales: Understanding and manipulating the crossover. Proc. Natl. Acad. Sci. USA. 102:9475-9480.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9475-9480
    • Rajamani, S.1    Truskett, T.2    Garde, S.3
  • 21
    • 0000899007 scopus 로고    scopus 로고
    • Cavity expulsion and weak dewetting of hydrophobic solutes in water
    • Hummer, G., and S. Garde. 1998. Cavity expulsion and weak dewetting of hydrophobic solutes in water. Phys. Rev. Lett. 80:4193-4196.
    • (1998) Phys. Rev. Lett , vol.80 , pp. 4193-4196
    • Hummer, G.1    Garde, S.2
  • 22
    • 0000067520 scopus 로고
    • Repulsion of interfaces due to boundary water
    • Marcelja, S., and N. Radic. 1976. Repulsion of interfaces due to boundary water. Chem. Phys. Lett. 42:129-130.
    • (1976) Chem. Phys. Lett , vol.42 , pp. 129-130
    • Marcelja, S.1    Radic, N.2
  • 24
    • 0000989338 scopus 로고    scopus 로고
    • Simple physical explanation of the unusual thermodynamic behavior of liquid water
    • Tanaka, H. 1998. Simple physical explanation of the unusual thermodynamic behavior of liquid water. Phys. Rev. Lett. 80:5750-5753.
    • (1998) Phys. Rev. Lett , vol.80 , pp. 5750-5753
    • Tanaka, H.1
  • 28
    • 33344476423 scopus 로고    scopus 로고
    • Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces
    • Cheung, M., and D. Thirumalai. 2006. Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces. J. Mol. Biol. 357:632-643.
    • (2006) J. Mol. Biol , vol.357 , pp. 632-643
    • Cheung, M.1    Thirumalai, D.2
  • 29
    • 0033515436 scopus 로고    scopus 로고
    • Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity
    • Betancourt, M., and D. Thirumalai. 1999. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. J. Mol. Biol. 287:627-644.
    • (1999) J. Mol. Biol , vol.287 , pp. 627-644
    • Betancourt, M.1    Thirumalai, D.2
  • 30
    • 0141482088 scopus 로고    scopus 로고
    • How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations
    • Takagi, F., N. Koga, and S. Takada. 2003. How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: molecular simulations. Proc. Natl. Acad. Sci. USA. 100:11367-11372.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11367-11372
    • Takagi, F.1    Koga, N.2    Takada, S.3
  • 31
    • 0043238073 scopus 로고    scopus 로고
    • Effects of confinement in chaperonin assisted protein folding: Rate enhancement by decreasing the roughness of the folding energy landscape
    • Baumketner, A., A. Jewett, and J. E. Shea. 2003. Effects of confinement in chaperonin assisted protein folding: rate enhancement by decreasing the roughness of the folding energy landscape. J. Mol. Biol. 332:701-713.
    • (2003) J. Mol. Biol , vol.332 , pp. 701-713
    • Baumketner, A.1    Jewett, A.2    Shea, J.E.3
  • 32
    • 4444330162 scopus 로고    scopus 로고
    • Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: Creation of an alternate fast folding pathway
    • Jewett, A. I., A. Baumketner, and J. E. Shea. 2004. Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway. Proc. Natl. Acad. Sci. USA. 101:13192-13197.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13192-13197
    • Jewett, A.I.1    Baumketner, A.2    Shea, J.E.3
  • 33
    • 0037117477 scopus 로고    scopus 로고
    • Unspecific hydrophobic stabilization of folding transition states
    • Viguera, A., C. Vega, and L. Serrano. 2002. Unspecific hydrophobic stabilization of folding transition states. Proc. Natl. Acad. Sci. USA. 99:5349-5354.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5349-5354
    • Viguera, A.1    Vega, C.2    Serrano, L.3
  • 34
    • 0036172116 scopus 로고    scopus 로고
    • Hydrophobic core packing in the SH3 domain folding transition state
    • Northey, J. G. B., A. Di Nardo, and A. R. Davidson. 2002. Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9:126-130.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 126-130
    • Northey, J.G.B.1    Di Nardo, A.2    Davidson, A.R.3
  • 35
    • 0038047129 scopus 로고    scopus 로고
    • Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding
    • Calloni, G., N. Taddei, K. Plaxco, G. Ramponi, M. Stefani, and F. Chiti. 2003. Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 330:577-591.
    • (2003) J. Mol. Biol , vol.330 , pp. 577-591
    • Calloni, G.1    Taddei, N.2    Plaxco, K.3    Ramponi, G.4    Stefani, M.5    Chiti, F.6
  • 37
    • 0032506017 scopus 로고    scopus 로고
    • Limited internal friction in the rate-limiting step of a two-state protein folding reaction
    • Plaxco, K., and D. Baker. 1998. Limited internal friction in the rate-limiting step of a two-state protein folding reaction. Proc. Natl. Acad. Sci. USA. 95:13591-13596.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13591-13596
    • Plaxco, K.1    Baker, D.2
  • 38
    • 0037423748 scopus 로고    scopus 로고
    • High concentrations of viscogens decrease the protein folding rate constant by prematurely collapsing the coil
    • Silow, M., and M. Oliveberg. 2003. High concentrations of viscogens decrease the protein folding rate constant by prematurely collapsing the coil. J. Mol. Biol. 326:263-271.
    • (2003) J. Mol. Biol , vol.326 , pp. 263-271
    • Silow, M.1    Oliveberg, M.2
  • 39
    • 0037184939 scopus 로고    scopus 로고
    • Directed evolution of substrate-optimized GroEL/S chaperonins
    • Wang, J. D., C. Herman, K. A. Tipton, C. A. Gross, and J. S. Weissman. 2002. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell. 111:1027-1039.
    • (2002) Cell , vol.111 , pp. 1027-1039
    • Wang, J.D.1    Herman, C.2    Tipton, K.A.3    Gross, C.A.4    Weissman, J.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.