메뉴 건너뛰기




Volumn 83, Issue 4, 2002, Pages 2219-2230

Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; DODECYL SULFATE SODIUM; PROTEIN; SODIUM CHLORIDE;

EID: 0036787578     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)73982-9     Document Type: Article
Times cited : (274)

References (43)
  • 1
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. 1996. How Hofmeister ion interactions affect protein stability. Biophys. J. 71:2056-2063.
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 4
    • 0036120608 scopus 로고    scopus 로고
    • Enthalpy-entropy compensation: A phantom phenomenon
    • Cornish-Bowden, A. 2002. Enthalpy-entropy compensation: a phantom phenomenon. J. Biosci. 27:121-126.
    • (2002) J. Biosci. , vol.27 , pp. 121-126
    • Cornish-Bowden, A.1
  • 5
    • 0001497127 scopus 로고
    • Influence of salt, detergent concentration and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecyl sulfate with m-dicyanobenzene
    • Croonen, Y., E. Geladé, M. Van der Zegel, M. Van der Auweraer, H. Vandendriessche. F. C. De Schryver. and M. Almgren. 1983. Influence of salt, detergent concentration and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecyl sulfate with m-dicyanobenzene. J. Phys. Chem. 87:1426-1431.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1426-1431
    • Croonen, Y.1    Geladé, E.2    Van der Zegel, M.3    Van der Auweraer, M.4    Vandendriessche, H.5    De Schryver, F.C.6    Almgren, M.7
  • 6
    • 0013893808 scopus 로고
    • The interaction of bovine plasma albumin with detergent anions. Stoichiometry and mechanism of binding of alkylbenzenesulfonates
    • Decker, R. V., and J. F. Foster. 1966. The interaction of bovine plasma albumin with detergent anions. Stoichiometry and mechanism of binding of alkylbenzenesulfonates. Biochemistry. 5:1242-1249.
    • (1966) Biochemistry , vol.5 , pp. 1242-1249
    • Decker, R.V.1    Foster, J.F.2
  • 9
    • 0024391087 scopus 로고
    • Lipid coumarin dye as a probe of interfacial electrical potential in biomembranes
    • Fromherz, P. 1989. Lipid coumarin dye as a probe of interfacial electrical potential in biomembranes. Methods Enzymol. 171:376-387.
    • (1989) Methods Enzymol. , vol.171 , pp. 376-387
    • Fromherz, P.1
  • 10
    • 11744264026 scopus 로고    scopus 로고
    • A light-scattering investigation of the sodium dodecyl sulfate-lysozyme system
    • Gimel, J. C., and W. Brown. 1996. A light-scattering investigation of the sodium dodecyl sulfate-lysozyme system. J. Chem. Phys. 104: 8112-8117.
    • (1996) J. Chem. Phys. , vol.104 , pp. 8112-8117
    • Gimel, J.C.1    Brown, W.2
  • 11
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen, S. J., J. Hofrichter, A. Szabo, and W. A. Eaton. 1996. Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. U. S. A. 93:11615-11617.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 13
    • 0025314149 scopus 로고
    • Protein-decorated micelle structure of sodium-dodecyl-sulfate-protein complexes as determined by neutron scattering
    • Ibel, K., R. P. May, K. Kirschner, H. Szadkowski, E. Mascher, and P. Lundahl. 1990. Protein-decorated micelle structure of sodium-dodecyl-sulfate-protein complexes as determined by neutron scattering. Eur. J. Biochem. 190:311-318.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 311-318
    • Ibel, K.1    May, R.P.2    Kirschner, K.3    Szadkowski, H.4    Mascher, E.5    Lundahl, P.6
  • 14
    • 0017123256 scopus 로고
    • Stepwise degradation of serum low density lipoprotein by sodium dodecyl sulfate
    • Ikai, A. 1976. Stepwise degradation of serum low density lipoprotein by sodium dodecyl sulfate. J. Biochem. 29:679-688.
    • (1976) J. Biochem. , vol.29 , pp. 679-688
    • Ikai, A.1
  • 15
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson, S. E., M. Moracci, N. elMasry, C. M. Johnson, and A. R. Fersht. 1993. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry. 32:11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    ElMasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 16
    • 0001285423 scopus 로고
    • Binding of n-alkyl sulphates to lysozyme in aqueous solution
    • Jones, M. N., and P. Manley. 1979. Binding of n-alkyl sulphates to lysozyme in aqueous solution. J. Chem. Soc. Faraday Trans. 75: 1736-1744.
    • (1979) J. Chem. Soc. Faraday Trans. , vol.75 , pp. 1736-1744
    • Jones, M.N.1    Manley, P.2
  • 17
    • 37049103647 scopus 로고
    • Interaction between lysozyme and n-alkyl sulfates in aqueous solution
    • Jones, M. N., and P. Manley. 1980. Interaction between lysozyme and n-alkyl sulfates in aqueous solution. J. Chem. Soc. Faraday. Trans. 76:654-664.
    • (1980) J. Chem. Soc. Faraday. Trans. , vol.76 , pp. 654-664
    • Jones, M.N.1    Manley, P.2
  • 18
    • 0016782741 scopus 로고
    • The interaction between bovine serum albumin and surfactants
    • Jones. M. N., H. A. Skinner, and E. Tipping. 1975. The interaction between bovine serum albumin and surfactants. Biochem. J. 147:229-234.
    • (1975) Biochem. J. , vol.147 , pp. 229-234
    • Jones, M.N.1    Skinner, H.A.2    Tipping, E.3
  • 19
    • 0015820894 scopus 로고
    • The interaction between ribonuclease A and surfactants
    • Jones, M. N., H. A. Skinner, E. Tipping, and A. Wilkinson. 1973. The interaction between ribonuclease A and surfactants. Biochem. J. 135: 231-236.
    • (1973) Biochem. J. , vol.135 , pp. 231-236
    • Jones, M.N.1    Skinner, H.A.2    Tipping, E.3    Wilkinson, A.4
  • 22
    • 0022673834 scopus 로고
    • Micellar aggregation numbers at high surfactant concentration
    • Malliaris, A., J. Lang, and R. Zana. 1986. Micellar aggregation numbers at high surfactant concentration. J. Colloid Interface Sci. 110:237-241.
    • (1986) J. Colloid Interface Sci. , vol.110 , pp. 237-241
    • Malliaris, A.1    Lang, J.2    Zana, R.3
  • 23
    • 0037181387 scopus 로고    scopus 로고
    • Measurement of electrostatic interactions in protein folding with the use of protein charge ladders
    • Negin, R. S., and J. D. Carbeck. 2002. Measurement of electrostatic interactions in protein folding with the use of protein charge ladders. J. Am. Chem. Soc. 124:2911-2916.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2911-2916
    • Negin, R.S.1    Carbeck, J.D.2
  • 24
    • 0016157537 scopus 로고
    • The interaction of a cationic detergent with bovine serum albumin and other proteins
    • Nozaki, Y., J. A. Reynolds, and C. Tanford. 1974. The interaction of a cationic detergent with bovine serum albumin and other proteins. J. Biol. Chem. 249:4452-4457.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4452-4457
    • Nozaki, Y.1    Reynolds, J.A.2    Tanford, C.3
  • 25
    • 0029670343 scopus 로고    scopus 로고
    • Formation of electrostatic interactions in the protein-folding pathway
    • Oliveberg, M., and A. R. Fersht. 1996. Formation of electrostatic interactions in the protein-folding pathway. Biochemistry. 35:2726-2737.
    • (1996) Biochemistry , vol.35 , pp. 2726-2737
    • Oliveberg, M.1    Fersht, A.R.2
  • 26
    • 0028981210 scopus 로고
    • Negative activation enthalpy in the kinetics of protein folding
    • Oliveberg, M., Y. J. Tan, and A. R. Fersht. 1995. Negative activation enthalpy in the kinetics of protein folding. Proc. Natl. Acad. Sci. U.S.A. 92:8926-8929.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.J.2    Fersht, A.R.3
  • 27
    • 0027980588 scopus 로고
    • Thermodynamic study of the acid denaturation of barnase and its dependence of ionic strength: Evidence for residual electrostatic interactions in the acid/thermally denatured state
    • Oliveberg, M., S. Vuilleumier, and A. R. Fersht. 1994. Thermodynamic study of the acid denaturation of barnase and its dependence of ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. Biochemistry. 33:8826-8832.
    • (1994) Biochemistry , vol.33 , pp. 8826-8832
    • Oliveberg, M.1    Vuilleumier, S.2    Fersht, A.R.3
  • 28
    • 0024977344 scopus 로고
    • NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide
    • O'Neil, J. D. J., and B. D. Sykes. 1989. NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide. Biochemistry. 28:699-797.
    • (1989) Biochemistry , vol.28 , pp. 699-797
    • O'Neil, J.D.J.1    Sykes, B.D.2
  • 29
    • 0032871869 scopus 로고    scopus 로고
    • A comparative study of the unfolding of EGV in denaturant and surfactant
    • Otzen, D. E., L. Christensen, and M. Schülein. 1999a. A comparative study of the unfolding of EGV in denaturant and surfactant. Protein Sci. 8:1878-1887.
    • (1999) Protein Sci. , vol.8 , pp. 1878-1887
    • Otzen, D.E.1    Christensen, L.2    Schülein, M.3
  • 30
    • 0033580679 scopus 로고    scopus 로고
    • Structural changes in the transition state of protein folding: An alternative interpretation of curved chevron plots
    • Otzen, D. E., O. Kristensen, M. Proctor, and M. Oliveberg. 1999b. Structural changes in the transition state of protein folding: an alternative interpretation of curved chevron plots. Biochemistry. 38:6499-6511.
    • (1999) Biochemistry , vol.38 , pp. 6499-6511
    • Otzen, D.E.1    Kristensen, O.2    Proctor, M.3    Oliveberg, M.4
  • 31
    • 0036307492 scopus 로고    scopus 로고
    • Burst-phase expansion of native protein prior to global unfolding in SDS
    • Otzen, D. E., and M. Oliveberg. 2002a. Burst-phase expansion of native protein prior to global unfolding in SDS. J. Mol. Biol. 315:1231-1240.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1231-1240
    • Otzen, D.E.1    Oliveberg, M.2
  • 32
    • 0036293485 scopus 로고    scopus 로고
    • Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state
    • Otzen, D. E., and M. Oliveberg. 2002b. Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state. J. Mol. Biol. 317:613-627.
    • (2002) J. Mol. Biol. , vol.317 , pp. 613-627
    • Otzen, D.E.1    Oliveberg, M.2
  • 33
    • 0014063229 scopus 로고
    • The binding of divers detergent anions to bovine serum albumin
    • Reynolds, J. A., S. Herbert, H. Polet, and J. Steinhardt. 1967. The binding of divers detergent anions to bovine serum albumin. Biochemistry. 6:937-943.
    • (1967) Biochemistry , vol.6 , pp. 937-943
    • Reynolds, J.A.1    Herbert, S.2    Polet, H.3    Steinhardt, J.4
  • 34
    • 0014940381 scopus 로고
    • The gross conformation of protein-sodium dodecyl sulfate complexes
    • Reynolds, J. A., and C. Tanford. 1970. The gross conformation of protein-sodium dodecyl sulfate complexes. J. Biol. Chem. 245:5161-5165.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5161-5165
    • Reynolds, J.A.1    Tanford, C.2
  • 36
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff. S. N. 1993. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22:67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 37
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. 1998. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51:355-432.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 38
    • 33751155438 scopus 로고
    • Spectroscopic probe analysis of protein-surfactant interactions: The BSA/SDS system
    • Turro, N. J., X.-G. Lei. K. P. Ananthapadmanabhan, and M. Aronson. 1995. Spectroscopic probe analysis of protein-surfactant interactions: the BSA/SDS system. Langmuir. 11:2525-2533.
    • (1995) Langmuir , vol.11 , pp. 2525-2533
    • Turro, N.J.1    Lei, X.-G.2    Ananthapadmanabhan, K.P.3    Aronson, M.4
  • 39
    • 0002664092 scopus 로고
    • Comparison of electrostatic- and hydrophobic-induced pKa shifts in polypentapeptides. The lysine residue
    • Urry, D. W., S. Peng, D. C. Gowda, T. M. Parker, and R. D. Harris. 1994. Comparison of electrostatic- and hydrophobic-induced pKa shifts in polypentapeptides. The lysine residue. Chem. Phys. Lett. 225:97-103.
    • (1994) Chem. Phys. Lett. , vol.225 , pp. 97-103
    • Urry, D.W.1    Peng, S.2    Gowda, D.C.3    Parker, T.M.4    Harris, R.D.5
  • 40
    • 0025932041 scopus 로고
    • A "molten-globule" membrane -insertion intermediate of the poreforming domain of colicin A
    • Van der Goot, F. G., J. M. Gonzalez-Manas, J. H. Lakey, and F. Pattus. 1991. A "molten-globule" membrane -insertion intermediate of the poreforming domain of colicin A. Nature. 354:408-410.
    • (1991) Nature , vol.354 , pp. 408-410
    • Van der Goot, F.G.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 42
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 43
    • 0017335799 scopus 로고
    • Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme
    • Yonath, A., A. Podjarny, B. Honig, A. Sielecki, and W. Traub. 1977. Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme. Biochemistry. 16:1418-1424.
    • (1977) Biochemistry , vol.16 , pp. 1418-1424
    • Yonath, A.1    Podjarny, A.2    Honig, B.3    Sielecki, A.4    Traub, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.