메뉴 건너뛰기




Volumn 84, Issue 6, 2003, Pages 3904-3916

Refolding of a high molecular weight protein: Salt effect on collapse

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOLYTE; FIBRONECTIN; POLYMER; SODIUM CHLORIDE; SOLVENT; UREA;

EID: 0038101552     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)75118-2     Document Type: Article
Times cited : (34)

References (42)
  • 1
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin, R. L., and G. D. Rose. 1999. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24: 77-83.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 2
    • 0001628801 scopus 로고    scopus 로고
    • Monte Carlo simulations of hydrophobic polyelectrolytes: Evidence of complete configurational transitions
    • Chodanowski, P., and S. Stoll. 1999. Monte Carlo simulations of hydrophobic polyelectrolytes: evidence of complete configurational transitions. J. Chem. Phys. 111:6069-6081.
    • (1999) J. Chem. Phys. , vol.111 , pp. 6069-6081
    • Chodanowski, P.1    Stoll, S.2
  • 6
    • 1842298212 scopus 로고    scopus 로고
    • From Leventhal to pathways to funnels
    • Dill, A. K., and H. S. Chan. 1997. From Leventhal to pathways to funnels. Nat. Struct. Biol. 4:10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, A.K.1    Chan, H.S.2
  • 7
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner, A. R., A. Sali, L. J. Smith, C. M. Dobson, and M. Karplus. 2000. Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem. Sci. 25:331-339.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 8
    • 0001189194 scopus 로고
    • Flory theory of a polyampholyte chain
    • Dobrynin, A., and M. Rubinstein. 1995. Flory theory of a polyampholyte chain. J. Phys. II France. 5:677-695.
    • (1995) J. Phys. II France , vol.5 , pp. 677-695
    • Dobrynin, A.1    Rubinstein, M.2
  • 9
    • 0030574963 scopus 로고    scopus 로고
    • Cascade transitions of polyelectrolytes in poor solvents
    • Dobrynin, A., M. Rubinstein, and S. Obukhov. 1996. Cascade transitions of polyelectrolytes in poor solvents. Macromolecules. 29:2974-2979.
    • (1996) Macromolecules , vol.29 , pp. 2974-2979
    • Dobrynin, A.1    Rubinstein, M.2    Obukhov, S.3
  • 10
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 11
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson, C. M., and M. Karplus. 1999. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9: 92-101.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 12
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis, R. J., and F. U. Hartl. 1999. Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 9:102-110.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 13
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht, A., and V. Daggett. 2002. Protein folding and unfolding at atomic resolution. Cell. 108:573-582.
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.1    Daggett, V.2
  • 14
    • 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
  • 16
    • 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
  • 18
    • 36449005109 scopus 로고
    • Theory of polyampholyte solutions
    • Higgs, P. G., and J.-F. Joanny. 1991. Theory of polyampholyte solutions. J. Chem. Phys. 94:1543-1554.
    • (1991) J. Chem. Phys. , vol.94 , pp. 1543-1554
    • Higgs, P.G.1    Joanny, J.-F.2
  • 19
    • 0032744232 scopus 로고    scopus 로고
    • Protein folding: From the Leventhal paradox to structure prediction
    • Honig, B. 1999. Protein folding: from the Leventhal paradox to structure prediction. J. Mol. Biol. 293:283-293.
    • (1999) J. Mol. Biol. , vol.293 , pp. 283-293
    • Honig, B.1
  • 20
    • 0035198044 scopus 로고    scopus 로고
    • Multiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturation
    • Hung, H., and G. Chang. 2001. Multiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturation. Biophys. J. 81:3456-3471.
    • (2001) Biophys. J. , vol.81 , pp. 3456-3471
    • Hung, H.1    Chang, G.2
  • 21
    • 0001339660 scopus 로고
    • The study of biological structures by neutron scattering from solution
    • Jacrot, B. 1976. The study of biological structures by neutron scattering from solution. Rep. Prog. Phys. 39:911-953.
    • (1976) Rep. Prog. Phys. , vol.39 , pp. 911-953
    • Jacrot, B.1
  • 22
    • 5744238033 scopus 로고
    • Instabilities of charged polyampholytes
    • Kantor, Y., and M. Kardar. 1995. Instabilities of charged polyampholytes. Phys. Rev. E. 51:1299-1312.
    • (1995) Phys. Rev. E , vol.51 , pp. 1299-1312
    • Kantor, Y.1    Kardar, M.2
  • 23
    • 0030324821 scopus 로고    scopus 로고
    • X-ray solution scattering studies of protein folding
    • Kataoka, M., and Y. Goto. 1996. X-ray solution scattering studies of protein folding. Fold. Des. 1:107-114.
    • (1996) Fold. Des. , vol.1 , pp. 107-114
    • Kataoka, M.1    Goto, Y.2
  • 24
    • 0345771649 scopus 로고    scopus 로고
    • Résolution d'un spectromètre de diffusion de neutrons aux petits angles
    • Lairez, D. 1999. Résolution d'un spectromètre de diffusion de neutrons aux petits angles. J. Phys. IV. 9:67-81.
    • (1999) J. Phys. IV , vol.9 , pp. 67-81
    • Lairez, D.1
  • 25
    • 0033852796 scopus 로고    scopus 로고
    • Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    • Pace, C., R. Alston, and K. Shaw. 2000. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Prot. Sci. 9:1395-1398.
    • (2000) Prot. Sci. , vol.9 , pp. 1395-1398
    • Pace, C.1    Alston, R.2    Shaw, K.3
  • 26
    • 0034338307 scopus 로고    scopus 로고
    • Heteropolymer freezing and design: Towards physical models of protein folding
    • Pande, V. S., A. Y. Grosberg, and T. Tanaka. 2000. Heteropolymer freezing and design: towards physical models of protein folding. Rev. Mod. Phys. 72:260-314.
    • (2000) Rev. Mod. Phys. , vol.72 , pp. 260-314
    • Pande, V.S.1    Grosberg, A.Y.2    Tanaka, T.3
  • 27
    • 0030569147 scopus 로고    scopus 로고
    • Scattering functions of semiflexible polymers with and without excluded volume effects
    • Pedersen, J. S., and P. Schurtenberger. 1996. Scattering functions of semiflexible polymers with and without excluded volume effects. Macromolecules. 29:7602-7612.
    • (1996) Macromolecules , vol.29 , pp. 7602-7612
    • Pedersen, J.S.1    Schurtenberger, P.2
  • 28
    • 0034595302 scopus 로고    scopus 로고
    • Statistical conformation of human plasma fibronectin
    • Pelta, J., H. Berry, G. C. Fadda, E. Pauthe, and D. Lairez. 2000. Statistical conformation of human plasma fibronectin. Biochemistry. 39:5146-5154.
    • (2000) Biochemistry , vol.39 , pp. 5146-5154
    • Pelta, J.1    Berry, H.2    Fadda, G.C.3    Pauthe, E.4    Lairez, D.5
  • 29
    • 0033212808 scopus 로고    scopus 로고
    • Plasma fibronectin: Three steps to purification and stability
    • Poulouin, L., O. Gallet, M. Rouahi, and J.-M. Imhoff. 1999. Plasma fibronectin: three steps to purification and stability. Prot. Expres. Purif. 17:146-152.
    • (1999) Prot. Expres. Purif. , vol.17 , pp. 146-152
    • Poulouin, L.1    Gallet, O.2    Rouahi, M.3    Imhoff, J.-M.4
  • 30
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. 1979. Stability of proteins: small globular proteins. Adv. Protein Chem. 33:167-236.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-236
    • Privalov, P.L.1
  • 31
    • 0033617266 scopus 로고    scopus 로고
    • From computer simulations to human disease: Emerging themes in protein folding
    • Radford, S., and C. M. Dobson. 1999. From computer simulations to human disease: emerging themes in protein folding. Cell. 97:291-298.
    • (1999) Cell , vol.97 , pp. 291-298
    • Radford, S.1    Dobson, C.M.2
  • 32
    • 0034383950 scopus 로고    scopus 로고
    • Protein folding: Progress made and promises ahead
    • Radford, S. E. 2000. Protein folding: progress made and promises ahead. Trends Biochem. Sci. 25:611-618.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 611-618
    • Radford, S.E.1
  • 33
    • 0023920076 scopus 로고
    • Fibronectin and its receptors
    • Ruoslahti, E. 1988. Fibronectin and its receptors. Annu. Rev. Biochem. 57:375-413.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 375-413
    • Ruoslahti, E.1
  • 35
    • 0035799343 scopus 로고    scopus 로고
    • Characterization of the denatured states distribution of neocarzinostatin by small-angle neutron scattering and differential scanning calorimetry
    • Russo, D., D. Durand, P. Calmettes, and M. Desmadril. 2001. Characterization of the denatured states distribution of neocarzinostatin by small-angle neutron scattering and differential scanning calorimetry. Biochemistry. 40:3958-3966.
    • (2001) Biochemistry , vol.40 , pp. 3958-3966
    • Russo, D.1    Durand, D.2    Calmettes, P.3    Desmadril, M.4
  • 36
    • 0033902504 scopus 로고    scopus 로고
    • Study of thermally and chemically unfolded conformations of a small β-protein by means of small-angle neutron scattering
    • Russo, D., D. Durand, M. Desmadril, and P. Calmettes. 2000. Study of thermally and chemically unfolded conformations of a small β-protein by means of small-angle neutron scattering. Phys. B. 276:520-521.
    • (2000) Phys. B , vol.276 , pp. 520-521
    • Russo, D.1    Durand, D.2    Desmadril, M.3    Calmettes, P.4
  • 37
    • 0001575397 scopus 로고    scopus 로고
    • Monte Carlo simulations and selfconsistent integral equation theory for polyelectrolyte solutions
    • Shew, C.-Y., and A. Yethiraj. 1999. Monte Carlo simulations and selfconsistent integral equation theory for polyelectrolyte solutions. J. Chem. Phys. 110:5437-5443.
    • (1999) J. Chem. Phys. , vol.110 , pp. 5437-5443
    • Shew, C.-Y.1    Yethiraj, A.2
  • 38
    • 0034324577 scopus 로고    scopus 로고
    • Self-consistent integral equation theory for semiflexible chain polyelectrolyte solutions
    • Shew, C.-Y., and A. Yethiraj. 2000. Self-consistent integral equation theory for semiflexible chain polyelectrolyte solutions. J. Chem. Phys. 113: 8841-8847.
    • (2000) J. Chem. Phys. , vol.113 , pp. 8841-8847
    • Shew, C.-Y.1    Yethiraj, A.2
  • 39
    • 36449001994 scopus 로고
    • The nature of flexible linear polyelectrolytes in salt free solution: A molecular dynamics study
    • Stevens, M. J., and K. Kremer. 1995. The nature of flexible linear polyelectrolytes in salt free solution: a molecular dynamics study. J. Chem. Phys. 103:1669-1690.
    • (1995) J. Chem. Phys. , vol.103 , pp. 1669-1690
    • Stevens, M.J.1    Kremer, K.2
  • 40
    • 0032512876 scopus 로고    scopus 로고
    • Solution structure of the glycosylated second type-II module of fibronectin
    • Sticht, H., A. Pickford, J. Potts, and I. Campbell. 1998. Solution structure of the glycosylated second type-II module of fibronectin. J. Mol. Biol. 276:177-187.
    • (1998) J. Mol. Biol. , vol.276 , pp. 177-187
    • Sticht, H.1    Pickford, A.2    Potts, J.3    Campbell, I.4
  • 41
    • 0028213715 scopus 로고
    • Solution structure of a pair of fibronectin type-I modules with fibrin binding-activity
    • Williams, M., I. Phan, T. Harvey, A. Rostagno, L. Gold, and I. Campbell. 1994. Solution structure of a pair of fibronectin type-I modules with fibrin binding-activity. J. Mol. Biol. 235:1302-1311.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1302-1311
    • Williams, M.1    Phan, I.2    Harvey, T.3    Rostagno, A.4    Gold, L.5    Campbell, I.6
  • 42
    • 0004133195 scopus 로고
    • Academic Press, New York
    • Yamada, K. 1989. Fibronectin. Academic Press, New York. pp. 48-121.
    • (1989) Fibronectin , pp. 48-121
    • Yamada, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.