메뉴 건너뛰기




Volumn 9, Issue 1, 2012, Pages

Effects of confinement on thermal stability and folding kinetics in a simple Ising-like model

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 84856948690     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/9/1/016006     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • DOI 10.1016/S0968-0004(01)01938-7, PII S0968000401019387
    • Ellis R J 2001 Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 597-604 (Pubitemid 32925190)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 597-604
    • Ellis, R.J.1
  • 2
    • 0031022118 scopus 로고    scopus 로고
    • Influence of excluded volume upon macromolecular structure and associations in 'crowded' media
    • DOI 10.1016/S0958-1669(97)80159-0
    • Minton A P 1997 Influence of excluded volume upon macromolecular structure and associations in 'crowded' media Curr. Opin. Biotechnol. 8 65-9 (Pubitemid 27067467)
    • (1997) Current Opinion in Biotechnology , vol.8 , Issue.1 , pp. 65-69
    • Minton, A.P.1
  • 3
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • DOI 10.1016/S0959-440X(99)00045-7
    • Minton A P 2000 Implication of macromolecular crowding for protein assembly Curr. Opin. Struct. Biol. 10 34-9 (Pubitemid 30099324)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 34-39
    • Minton, A.P.1
  • 4
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • DOI 10.1016/S0959-440X(00)00172-X
    • Ellis R J 2001 Macromolecular crowding: an important but neglected aspect of the intracellular environment Curr. Opin. Struct. Biol. 11 114-9 (Pubitemid 32155560)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.1 , pp. 114-119
    • Ellis, R.J.1
  • 5
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman S B and Trach S O 1991 Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli J. Mol. Biol. 222 599-620
    • (1991) J. Mol. Biol. , vol.222 , Issue.3 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 7
    • 79551687316 scopus 로고    scopus 로고
    • Protein folding in the cell: Challenges and progress
    • Gershenson A and Gierasch L M 2011 Protein folding in the cell: challenges and progress Curr. Opin. Struct. Biol. 21 32-41
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , Issue.1 , pp. 32-41
    • Gershenson, A.1    Gierasch, L.M.2
  • 8
    • 0035092041 scopus 로고    scopus 로고
    • Molecular confinement influences protein structure and enhances thermal protein stability
    • DOI 10.1110/ps.36201
    • Eggers D and Valentine J S 2001 Molecular confinement influences protein structure and enhances thermal protein stability Protein Sci. 10 250-61 (Pubitemid 32229119)
    • (2001) Protein Science , vol.10 , Issue.2 , pp. 250-261
    • Eggers, D.K.1    Valentine, J.S.2
  • 9
    • 16344373103 scopus 로고    scopus 로고
    • Unfolding of Green Fluorescent Protein mut2 in wet nanoporous silica gels
    • DOI 10.1110/ps.041190805
    • Campanini B, Bologna S, Cannone F, Chirico G, Mozzarelli A and Bettati S 2005 Unfolding of green fluorescent protein mut2 in wet nanoporous silica gels Protein Sci. 14 1125-33 (Pubitemid 40577792)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1125-1133
    • Campanini, B.1    Bologna, S.2    Cannone, F.3    Chirico, G.4    Mozzarelli, A.5    Bettati, S.6
  • 10
    • 4644332696 scopus 로고    scopus 로고
    • Protein encapsulation in mesoporous silicate: The effects of confinement on protein stability, hydration, and volumetric properties
    • DOI 10.1021/ja046900n
    • Ravindra R, Zhao S, Gies H and Winter R 2004 Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration and volumetric properties J. Am. Chem. Soc. 126 12224-5 (Pubitemid 39304879)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.39 , pp. 12224-12225
    • Ravindra, R.1    Zhao, S.2    Gies, H.3    Winter, R.4
  • 11
    • 0347130909 scopus 로고    scopus 로고
    • Protein Stability in Nanocages: A Novel Approach for Influencing Protein Stability by Molecular Confinement
    • DOI 10.1016/j.jmb.2003.11.056
    • Bolis D, Politou A S, Kelly G, Pastore A and Temussi P A 2004 Protein stability in nanocages: a novel approach for influencing protein stability by molecular confinement J. Mol. Biol. 336 203-12 (Pubitemid 38102342)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.1 , pp. 203-212
    • Bolis, D.1    Politou, A.S.2    Kelly, G.3    Pastore, A.4    Andrea Temussi, P.5
  • 12
    • 77955044557 scopus 로고    scopus 로고
    • Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state
    • Hong J and Gierasch L M 2010 Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state J. Am. Chem. Soc. 132 10445-52
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.30 , pp. 10445-10452
    • Hong, J.1    Gierasch, L.M.2
  • 13
    • 4544278751 scopus 로고    scopus 로고
    • Protein folding and binding in confined spaces and in crowded solutions
    • Zhou H X 2004 Protein folding and binding in confined spaces and in crowded solutions J. Mol. Recognit. 17 368-75
    • (2004) J. Mol. Recognit. , vol.17 , Issue.5 , pp. 368-375
    • Zhou, H.X.1
  • 14
    • 36749103188 scopus 로고    scopus 로고
    • Protein folding in confined and crowded environments
    • Zhou H X 2008 Protein folding in confined and crowded environments Arch. Biochem. Biophys. 469 76-82
    • (2008) Arch. Biochem. Biophys. , vol.469 , Issue.1 , pp. 76-82
    • Zhou, H.X.1
  • 18
    • 58149498257 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of protein folding under confinement
    • Mittal J and Best R B 2008 Thermodynamics and kinetics of protein folding under confinement Proc. Natl Acad. Sci. USA 105 20233-8
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.51 , pp. 20233-20238
    • Mittal, J.1    Best, R.B.2
  • 19
    • 33750720952 scopus 로고    scopus 로고
    • A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding
    • DOI 10.1021/bi061597j
    • Hayer-Hartl M and Minton A P 2006 A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding Biochemistry 45 13356-60 (Pubitemid 44707695)
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13356-13360
    • Hayer-Hartl, M.1    Minton, A.P.2
  • 21
    • 33645958276 scopus 로고    scopus 로고
    • Polymer chains in confined spaces and flow-injection problems: Some remarks
    • Sakaue T and Raphal E 2006 Polymer chains in confined spaces and flow-injection problems: some remarks Macromolecules 39 2621-8
    • (2006) Macromolecules , vol.39 , Issue.7 , pp. 2621-2628
    • Sakaue, T.1    Raphal, E.2
  • 23
    • 2042473511 scopus 로고
    • Statistical mechanical theory of the protein conformation: I. General considerations and the application to homopolymers
    • Wako H and Sait N 1978 Statistical mechanical theory of the protein conformation: I. General considerations and the application to homopolymers J. Phys. Soc. Japan 44 1931-9
    • (1978) J. Phys. Soc. Japan , vol.44 , Issue.6 , pp. 1931-1939
    • Wako, H.1    Sait, N.2
  • 24
    • 2042474146 scopus 로고
    • Statistical mechanical theory of the protein conformation: II. Folding pathway for protein
    • Wako H and Sait N 1978 Statistical mechanical theory of the protein conformation: II. Folding pathway for protein J. Phys. Soc. Japan 44 1939-45
    • (1978) J. Phys. Soc. Japan , vol.44 , Issue.6 , pp. 1939-1945
    • Wako, H.1    Sait, N.2
  • 25
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • DOI 10.1038/36626
    • Mũoz V, Thompson P A, Hofrichter J and Eaton W A 1997 Folding dynamics and mechanism of β-hairpin formation Nature 390 196-9 (Pubitemid 27507992)
    • (1997) Nature , vol.390 , Issue.6656 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 28
    • 0037166875 scopus 로고    scopus 로고
    • Exact solution of the Mũoz-Eaton model for protein folding
    • Bruscolini P and Pelizzola A 2002 Exact solution of the Mũoz-Eaton model for protein folding Phys. Rev. Lett. 88 258101
    • (2002) Phys. Rev. Lett. , vol.88 , Issue.25 , pp. 258101
    • Bruscolini, P.1    Pelizzola, A.2
  • 29
    • 29044435564 scopus 로고    scopus 로고
    • Exactness of the cluster variation method and factorization of the equilibrium probability for the Wako-Sait-Mũoz-Eaton model of protein folding
    • Pelizzola A 2005 Exactness of the cluster variation method and factorization of the equilibrium probability for the Wako-Sait-Mũoz-Eaton model of protein folding J. Stat. Mech. P11010
    • (2005) J. Stat. Mech. , vol.2005 , Issue.11 , pp. 11010
    • Pelizzola, A.1
  • 30
    • 33747133668 scopus 로고    scopus 로고
    • Kinetics of the Wako-Sait-Mũoz-Eaton model of protein folding
    • Zamparo M and Pelizzola A 2006 Kinetics of the Wako-Sait-Mũoz-Eaton model of protein folding Phys. Rev. Lett. 97 068106
    • (2006) Phys. Rev. Lett. , vol.97 , Issue.6 , pp. 068106
    • Zamparo, M.1    Pelizzola, A.2
  • 31
    • 42749099473 scopus 로고    scopus 로고
    • Rigorous results on the local equilibrium kinetics of a protein folding model
    • Zamparo M and Pelizzola A 2006 Rigorous results on the local equilibrium kinetics of a protein folding model J. Stat. Mech. P12009
    • (2006) J. Stat. Mech. , vol.2006 , Issue.12 , pp. 12009
    • Zamparo, M.1    Pelizzola, A.2
  • 32
    • 34250012657 scopus 로고    scopus 로고
    • Downhill versus two-state protein folding in a statistical mechanical model
    • Bruscolini P, Pelizzola A and Zamparo M 2007 Downhill versus two-state protein folding in a statistical mechanical model J. Chem. Phys. 126 215103
    • (2007) J. Chem. Phys. , vol.126 , Issue.21 , pp. 215103
    • Bruscolini, P.1    Pelizzola, A.2    Zamparo, M.3
  • 33
    • 34547178815 scopus 로고    scopus 로고
    • Rate determining factors in protein model structures
    • Bruscolini P, Pelizzola A and Zamparo M 2007 Rate determining factors in protein model structures Phys. Rev. Lett. 99 038103
    • (2007) Phys. Rev. Lett. , vol.99 , Issue.3 , pp. 038103
    • Bruscolini, P.1    Pelizzola, A.2    Zamparo, M.3
  • 34
    • 34147147538 scopus 로고    scopus 로고
    • Ising-like model for protein mechanical unfolding
    • Imparato A, Pelizzola A and Zamparo M 2007 Ising-like model for protein mechanical unfolding Phys. Rev. Lett. 98 148102
    • (2007) Phys. Rev. Lett. , vol.98 , Issue.14 , pp. 148102
    • Imparato, A.1    Pelizzola, A.2    Zamparo, M.3
  • 35
    • 35248849406 scopus 로고    scopus 로고
    • Protein mechanical unfolding: A model with binary variables
    • Imparato A, Pelizzola A and Zamparo M 2007 Protein mechanical unfolding: a model with binary variables J. Chem. Phys. 127 145105
    • (2007) J. Chem. Phys. , vol.127 , Issue.14 , pp. 145105
    • Imparato, A.1    Pelizzola, A.2    Zamparo, M.3
  • 36
    • 42449140300 scopus 로고    scopus 로고
    • Mechanical unfolding and refolding pathways of ubiquitin
    • Imparato A and Pelizzola A 2008 Mechanical unfolding and refolding pathways of ubiquitin Phys. Rev. Lett. 100 158104
    • (2008) Phys. Rev. Lett. , vol.100 , Issue.15 , pp. 158104
    • Imparato, A.1    Pelizzola, A.2
  • 37
    • 70350532400 scopus 로고    scopus 로고
    • Equilibrium properties and force-driven unfolding pathways of RNA molecules
    • Imparato A, Pelizzola A and Zamparo M 2009 Equilibrium properties and force-driven unfolding pathways of RNA molecules Phys. Rev. Lett. 103 188102
    • (2009) Phys. Rev. Lett. , vol.103 , Issue.18 , pp. 188102
    • Imparato, A.1    Pelizzola, A.2    Zamparo, M.3
  • 39
    • 80051608117 scopus 로고    scopus 로고
    • Direction dependent mechanical unfolding and green fluorescent protein as a force sensor
    • Caraglio M, Imparato A and Pelizzola A 2011 Direction dependent mechanical unfolding and green fluorescent protein as a force sensor Phys. Rev. E 84 021918
    • (2011) Phys. Rev. , vol.84 , Issue.2 , pp. 021918
    • Caraglio, M.1    Imparato, A.2    Pelizzola, A.3
  • 40
    • 79951900584 scopus 로고    scopus 로고
    • Analysis of the equilibrium and kinetics of the ankyrin repeat protein myotrophin
    • Faccin M, Bruscolini P and Pelizzola A 2011 Analysis of the equilibrium and kinetics of the ankyrin repeat protein myotrophin J. Chem. Phys. 134 075102
    • (2011) J. Chem. Phys. , vol.134 , Issue.7 , pp. 075102
    • Faccin, M.1    Bruscolini, P.2    Pelizzola, A.3
  • 41
    • 33646897305 scopus 로고    scopus 로고
    • Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein
    • DOI 10.1016/j.cell.2006.04.027, PII S0092867406005605
    • Tang Y-C, Chang H-C, Roeben A, Wischnewski D, Wischnewski N, Kerner M J, Hartl F U and Hayer-Hartl M 2006 Structural features of the groEL-groES nano-cage required for rapid folding of encapsulated protein Cell 125 903-14 (Pubitemid 43795198)
    • (2006) Cell , vol.125 , Issue.5 , pp. 903-914
    • Tang, Y.-C.1    Chang, H.-C.2    Roeben, A.3    Wischnewski, D.4    Wischnewski, N.5    Kerner, M.J.6    Hartl, F.U.7    Hayer-Hartl, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.