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Volumn 96, Issue 5, 2009, Pages 1892-1901

Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: Experiments and numerical simulations

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; GLYCINE; NUCLEOCAPSID PROTEIN; SODIUM CHLORIDE; SODIUM DIHYDROGEN PHOSPHATE; NUCLEOCAPSID PROTEIN, CORONAVIRUS; RNA;

EID: 65549118368     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.10.045     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0037561920 scopus 로고    scopus 로고
    • Characterization of a novel coronavirus associated with severe acute respiratory syndrome
    • Rota, P. A., M. S. Oberste, S. S. Monroe, W. A. Nix, R. Campagnoli, et al. 2003. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science. 300:1394-1399.
    • (2003) Science , vol.300 , pp. 1394-1399
    • Rota, P.A.1    Oberste, M.S.2    Monroe, S.S.3    Nix, W.A.4    Campagnoli, R.5
  • 3
    • 6344222994 scopus 로고    scopus 로고
    • In vitro biochemical and thermodynamical characterization of nucleocapsid protein of SARS
    • Luo, H., F. Ye, T. Sun, L. Yue, S. Peng, et al. 2004. In vitro biochemical and thermodynamical characterization of nucleocapsid protein of SARS. Biophys. Chem. 112:15-25.
    • (2004) Biophys. Chem , vol.112 , pp. 15-25
    • Luo, H.1    Ye, F.2    Sun, T.3    Yue, L.4    Peng, S.5
  • 4
    • 4644247362 scopus 로고    scopus 로고
    • Low stability of nucleocapsid protein in SARS virus
    • Wang, Y., X. Wu, Y. Wang, B. Li, H. Zhou, et al. 2004. Low stability of nucleocapsid protein in SARS virus. Biochemistry. 43:11103-11108.
    • (2004) Biochemistry , vol.43 , pp. 11103-11108
    • Wang, Y.1    Wu, X.2    Wang, Y.3    Li, B.4    Zhou, H.5
  • 5
    • 0242361262 scopus 로고    scopus 로고
    • Stability of SARS coronavirus in human specimen and environment and its sensitivity to heating and UV irradiation
    • Duan, S. M., X. S. Zhao, R. F. Wen, J. J. Huang, G. H. Pi, et al. 2003. Stability of SARS coronavirus in human specimen and environment and its sensitivity to heating and UV irradiation. Biomed. Environ. Sci. 16:105-111.
    • (2003) Biomed. Environ. Sci , vol.16 , pp. 105-111
    • Duan, S.M.1    Zhao, X.S.2    Wen, R.F.3    Huang, J.J.4    Pi, G.H.5
  • 7
    • 27644584130 scopus 로고    scopus 로고
    • Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent
    • Hsieh, P. K., S. C. Chang, C. C. Huang, T. T. Lee, C. W. Hsiao, et al. 2005. Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent. J. Virol. 79:13848-13855.
    • (2005) J. Virol , vol.79 , pp. 13848-13855
    • Hsieh, P.K.1    Chang, S.C.2    Huang, C.C.3    Lee, T.T.4    Hsiao, C.W.5
  • 8
    • 34147113199 scopus 로고    scopus 로고
    • Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA
    • Chen, C.-Y., C.-k. Chang, Y.-W. Chang, S.-C. Sue, H.-I. Bai, et al. 2007. Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA. J. Mol. Biol. 368:1075-1086.
    • (2007) J. Mol. Biol , vol.368 , pp. 1075-1086
    • Chen, C.-Y.1    Chang, C.-K.2    Chang, Y.-W.3    Sue, S.-C.4    Bai, H.-I.5
  • 9
    • 85031352949 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 11
    • 0014959662 scopus 로고
    • A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives
    • Tsong, T.-Y., R. P. Hearn, D. P. Wrathall, and J. M. Sturtevant. 1970. A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives. Biochemistry. 9:2666-2677.
    • (1970) Biochemistry , vol.9 , pp. 2666-2677
    • Tsong, T.-Y.1    Hearn, R.P.2    Wrathall, D.P.3    Sturtevant, J.M.4
  • 12
    • 46849118765 scopus 로고    scopus 로고
    • Hydrophobic condensation and modular assembly model of protein folding
    • Tsong, T.-Y., C.-K. Hu, and M.-C. Wu. 2008. Hydrophobic condensation and modular assembly model of protein folding. Biosystems. 93:78-89.
    • (2008) Biosystems , vol.93 , pp. 78-89
    • Tsong, T.-Y.1    Hu, C.-K.2    Wu, M.-C.3
  • 13
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō, N. 1983. Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12:183-210.
    • (1983) Annu. Rev. Biophys. Bioeng , vol.12 , pp. 183-210
    • Gō, N.1
  • 14
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural detail of transition state ensemble and en-route intermediates for protein folding? An investigation for small globular proteins
    • Clementi, C., H. Nymeyer, and J. N. Onuchic. 2000. Topological and energetic factors: what determines the structural detail of transition state ensemble and en-route intermediates for protein folding? An investigation for small globular proteins. J. Mol. Biol. 298:937-953.
    • (2000) J. Mol. Biol , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 15
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M., and R. H. Swendsen. 1989. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63:1195-1198.
    • (1989) Phys. Rev. Lett , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 16
    • 84984548144 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndrome coronavirus genomes in Taiwan: Molecular epidemiology and genome evolution
    • Yeh, S.-H., H.-Y. Wang, C.-Y. Tsai, C.-L. Kao, J.-Y. Yang, et al. 2004. Characterization of severe acute respiratory syndrome coronavirus genomes in Taiwan: molecular epidemiology and genome evolution. Proc. Natl. Acad. Sci. USA. 101:2542-2547.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2542-2547
    • Yeh, S.-H.1    Wang, H.-Y.2    Tsai, C.-Y.3    Kao, C.-L.4    Yang, J.-Y.5
  • 17
    • 26844453741 scopus 로고    scopus 로고
    • The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome viruslike structure
    • Chang, C.-k., S.-C. Sue, T.-H. Yu, C.-M. Hsieh, C.-K. Tsai, et al. 2005. The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome viruslike structure. FEBS Lett. 579:5663-5668.
    • (2005) FEBS Lett , vol.579 , pp. 5663-5668
    • Chang, C.-K.1    Sue, S.-C.2    Yu, T.-H.3    Hsieh, C.-M.4    Tsai, C.-K.5
  • 19
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
    • Schwarzinger, S., G. J. Kroon, T. R. Foss, P. E. Wright, and H. J. Dyson. 2000. Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J. Biomol. NMR. 18:43-48.
    • (2000) J. Biomol. NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 21
    • 0032742688 scopus 로고    scopus 로고
    • Gō-ing for the prediction of protein folding mechanisms
    • Takada, S. 1999. Gō-ing for the prediction of protein folding mechanisms. Proc. Natl. Acad. Sci. USA. 96:11698-11700.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11698-11700
    • Takada, S.1
  • 24
    • 30444455738 scopus 로고    scopus 로고
    • Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions
    • Li, M.-S., C.-K. Hu, D. K. Klimov, and D. Thirumalai. 2006. Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions. Proc. Natl. Acad. Sci. USA. 103:93-98.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 93-98
    • Li, M.-S.1    Hu, C.-K.2    Klimov, D.K.3    Thirumalai, D.4
  • 25
    • 38849169933 scopus 로고    scopus 로고
    • New force replica exchange method and protein folding pathways probed by force-clamp technique
    • Kouza, M., C.-K. Hu, and M. S. Li. 2008. New force replica exchange method and protein folding pathways probed by force-clamp technique. J. Chem. Phys. 128:045103.
    • (2008) J. Chem. Phys , vol.128 , pp. 045103
    • Kouza, M.1    Hu, C.-K.2    Li, M.S.3
  • 26
    • 36749110571 scopus 로고
    • Computer simulation method for the calculation of equilibrium constants for the formation of physical clusters and molecules: Application to small water clusters
    • Swope, W. C., H. C. Andersen, P. H. Berens, and K. R. Wilson. 1982. Computer simulation method for the calculation of equilibrium constants for the formation of physical clusters and molecules: application to small water clusters. J. Chem. Phys. 76:637-649.
    • (1982) J. Chem. Phys , vol.76 , pp. 637-649
    • Swope, W.C.1    Andersen, H.C.2    Berens, P.H.3    Wilson, K.R.4
  • 27
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties
    • Veitshans, T., D. K. Klimov, and D. Thirumalai. 1997. Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties. Fold. Des. 2:1-22.
    • (1997) Fold. Des , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.K.2    Thirumalai, D.3
  • 28
    • 33846460423 scopus 로고    scopus 로고
    • Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin
    • Li, M. S., M. Kouza, and C.-K. Hu. 2007. Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin. Biophys. J. 92:547-561.
    • (2007) Biophys. J , vol.92 , pp. 547-561
    • Li, M.S.1    Kouza, M.2    Hu, C.-K.3
  • 29
    • 0347123330 scopus 로고    scopus 로고
    • Thermal denaturation and folding rates of single domain proteins: Size matters
    • Li, M. S., D. K. Klimov, and D. Thirumalai. 2004. Thermal denaturation and folding rates of single domain proteins: size matters. Polymer (Guildf.). 45:573-579.
    • (2004) Polymer (Guildf.) , vol.45 , pp. 573-579
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 30
    • 42749106226 scopus 로고    scopus 로고
    • Finite size effects on thermal denaturation of globular proteins
    • Li, M. S., D. K. Klimov, and D. Thirumalai. 2004. Finite size effects on thermal denaturation of globular proteins. Phys. Rev. Lett. 93:268107.
    • (2004) Phys. Rev. Lett , vol.93 , pp. 268107
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 31
    • 14644442376 scopus 로고    scopus 로고
    • Finite size effects on calorimetric cooperativity of two-state proteins
    • Li, M. S., D. K. Klimov, and D. Thirumalai. 2005. Finite size effects on calorimetric cooperativity of two-state proteins. Physica A. 350:38-44.
    • (2005) Physica A , vol.350 , pp. 38-44
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 32
    • 31544472338 scopus 로고    scopus 로고
    • Effect of finite size on cooperativity and folding rates of proteins
    • Kouza, M., M. S. Li, C.-K. Hu, E. P. O'Brien, Jr., and D. Thirumalai. 2006. Effect of finite size on cooperativity and folding rates of proteins. J. Phys. Chem. A. 110:671-676.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 671-676
    • Kouza, M.1    Li, M.S.2    Hu, C.-K.3    O'Brien Jr., E.P.4    Thirumalai, D.5
  • 33
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chainlength scaling in protein folding: A simulation study with a Gō-like model
    • Koga, K., and S. Takaga. 2001. Roles of native topology and chainlength scaling in protein folding: a simulation study with a Gō-like model. J. Mol. Biol. 313:171-180.
    • (2001) J. Mol. Biol , vol.313 , pp. 171-180
    • Koga, K.1    Takaga, S.2
  • 35
    • 31544448267 scopus 로고    scopus 로고
    • An enhanced version of SMMP - open-source software package for simulation of proteins
    • Eisenmenger, F., U. H. E. Hansmann, S. Hayryan, and C.-K. Hu. 2006. An enhanced version of SMMP - open-source software package for simulation of proteins. Comp. Phys. Commun. 174:422-429.
    • (2006) Comp. Phys. Commun , vol.174 , pp. 422-429
    • Eisenmenger, F.1    Hansmann, U.H.E.2    Hayryan, S.3    Hu, C.-K.4
  • 37
    • 28644431872 scopus 로고    scopus 로고
    • Free energy landscape and folding mechanism of a β-hairpin in explicit water: A replica exchange molecular dynamics study
    • Nguyen, P. H., G. Stock, E. Mittag, C.-K. Hu, and M. S. Li. 2005. Free energy landscape and folding mechanism of a β-hairpin in explicit water: a replica exchange molecular dynamics study. Proteins: Struct. Funct. Bioinf. 61:795-808.
    • (2005) Proteins: Struct. Funct. Bioinf , vol.61 , pp. 795-808
    • Nguyen, P.H.1    Stock, G.2    Mittag, E.3    Hu, C.-K.4    Li, M.S.5
  • 38
    • 33847656545 scopus 로고    scopus 로고
    • Efficient combination of Wang-Landau and transition matrix Monte Carlo methods for protein simulations
    • Ghulghazaryan, R. G., S. Hayryan, and C.-K. Hu. 2007. Efficient combination of Wang-Landau and transition matrix Monte Carlo methods for protein simulations. J. Comp. Chem. 28:715-726.
    • (2007) J. Comp. Chem , vol.28 , pp. 715-726
    • Ghulghazaryan, R.G.1    Hayryan, S.2    Hu, C.-K.3


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