메뉴 건너뛰기




Volumn 278, Issue 4, 1998, Pages 879-894

Anion-induced folding of staphylococcal nuclease: Characterization of multiple equilibrium partially folded intermediates

Author keywords

A states; Molten globule; Protein folding; Small angle X ray scattering

Indexed keywords

ANION; BACTERIAL ENZYME; CHLORIDE; NUCLEASE; SULFATE; TRIFLUOROACETIC ACID; UREA;

EID: 0032525256     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1741     Document Type: Article
Times cited : (121)

References (62)
  • 1
    • 0014730026 scopus 로고
    • Analytical gel chromatography of proteins
    • Ackers G.L. Analytical gel chromatography of proteins. Advan. Protein Chem. 24:1970;343-446
    • (1970) Advan. Protein Chem. , vol.24 , pp. 343-446
    • Ackers, G.L.1
  • 2
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler A.J., Greenfield N.J., Fasman G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27:1973;675-735
    • (1973) Methods Enzymol , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 4
    • 0000992692 scopus 로고
    • Molten globule: Specific or nonspecific folding intermediates?
    • Baldwin R.L. Molten globule specific or nonspecific folding intermediates? Chemtracts-Biochem. Mol. Biol. 2:1991;379-389
    • (1991) Chemtracts-Biochem. Mol. Biol. , vol.2 , pp. 379-389
    • Baldwin, R.L.1
  • 5
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new
    • Baldwin R.L. The nature of protein folding pathways The classical versus the new. J. Biomol. NMR. 5:1995;103-109
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 6
    • 0026534194 scopus 로고
    • PH-induced folding/unfolding of staphylococcal nuclease: Determination of kinetic parameters by the sequential-jump method
    • Chen H.M., Markin V.S., Tsong T.Y. PH-induced folding/unfolding of staphylococcal nuclease determination of kinetic parameters by the sequential-jump method. Biochemistry. 31:1992;1483-1491
    • (1992) Biochemistry , vol.31 , pp. 1483-1491
    • Chen, H.M.1    Markin, V.S.2    Tsong, T.Y.3
  • 7
    • 0025982146 scopus 로고
    • Molten globule intermediates and protein folding
    • Christensen H., Pain R.H. Molten globule intermediates and protein folding. Eur. Biophys. J. 19:1991;221-229
    • (1991) Eur. Biophys. J. , vol.19 , pp. 221-229
    • Christensen, H.1    Pain, R.H.2
  • 8
    • 0021759423 scopus 로고
    • Use of high-speed size-exclusion chromatography for the study of protein folding and stability
    • Corbett R.J.T., Roche R.S. Use of high-speed size-exclusion chromatography for the study of protein folding and stability. Biochemistry. 23:1984;1888-1894
    • (1984) Biochemistry , vol.23 , pp. 1888-1894
    • Corbett, R.J.T.1    Roche, R.S.2
  • 9
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 10
    • 0001931668 scopus 로고
    • Unfolded proteins, compact states and molten globules
    • Dobson C.M. Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2:1992;6-12
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 6-12
    • Dobson, C.M.1
  • 11
    • 0029562577 scopus 로고
    • Partially folded states of proteins: Characterization by X-ray scattering
    • Doniach S., Bascle J., Garel T., Orland H. Partially folded states of proteins characterization by X-ray scattering. J. Mol. Biol. 254:1995;960-967
    • (1995) J. Mol. Biol. , vol.254 , pp. 960-967
    • Doniach, S.1    Bascle, J.2    Garel, T.3    Orland, H.4
  • 12
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink M.R., Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114:1981;199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 15
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink A.L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 16
    • 0027241814 scopus 로고
    • Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
    • Fink A.L., Calciano L.J., Goto Y., Nishimura M., Swedberg S.A. Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Sci. 2:1993;1155-1160
    • (1993) Protein Sci. , vol.2 , pp. 1155-1160
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Nishimura, M.4    Swedberg, S.A.5
  • 17
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink A.L., Calciano L.J., Goto Y., Kurotsu T., Palleros D.R. Classification of acid denaturation of proteins intermediates and unfolded states. Biochemistry. 33:1994;12504-12511
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 18
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates vs. molten globule models of protein folding: Characterization of partially folded intermediates of apomyoglobin
    • Fink A.L., Seshadri S., Oberg K.A. Discrete intermediates vs. molten globule models of protein folding Characterization of partially folded intermediates of apomyoglobin. Folding Design. 3:1997;19-25
    • (1997) Folding Design , vol.3 , pp. 19-25
    • Fink, A.L.1    Seshadri, S.2    Oberg, K.A.3
  • 19
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. 1. paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie J.R., Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. 1. paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268:1997;158-169
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 20
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. 2. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie J.R., Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. 2. distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268:1997;170-184
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 22
    • 0024963570 scopus 로고
    • Conformational states of β-lactamase: Molten globule states at acidic and alkaline pH with high salt
    • Goto Y., Fink A.L. Conformational states of β-lactamase molten globule states at acidic and alkaline pH with high salt. Biochemistry. 28:1989;945-952
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 24
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y., Takahashi N., Fink A.L. Mechanism of acid-induced folding of proteins. Biochemistry. 29:1990;3480-3488
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 25
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
    • Hamada D., Segawa S., Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nature Struct. Biol. 3:1996;868-873
    • (1996) Nature Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 26
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric lambda repressor
    • Huang G.S., Oas T.G. Submillisecond folding of monomeric lambda repressor. Proc. Nat. Acad. Sci. USA. 92:1995;6878-6882
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 27
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 28
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of alpha-lactalbumin and lysozyme
    • Ikeguchi M., Kuwajima K., Mitani M., Sugai S. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate a comparative study of the folding reactions of alpha-lactalbumin and lysozyme. Biochemistry. 25:1986;6965-6972
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 29
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 30
    • 0028832610 scopus 로고
    • Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism
    • Kalnin N.N., Kuwajima K. Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism. Proteins: Struct. Funct. Genet. 23:1995;163-176
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 163-176
    • Kalnin, N.N.1    Kuwajima, K.2
  • 31
    • 0000739195 scopus 로고
    • Melittin binding causes a large calcium-dependent conformational change in calmodulin
    • Kataoka M., Head J.F., Seaton B.A., Engelman D.M. Melittin binding causes a large calcium-dependent conformational change in calmodulin. Proc. Natl Acad. Sci. USA. 86:1989;6944-6948
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6944-6948
    • Kataoka, M.1    Head, J.F.2    Seaton, B.A.3    Engelman, D.M.4
  • 32
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by small angle X-ray scattering
    • Kataoka M., Hagihara Y., Mihara K., Goto Y. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229:1993;591-596
    • (1993) J. Mol. Biol. , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 33
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P.S., Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 34
    • 0024417964 scopus 로고
    • The molten globule as a clue for understanding the folding and cooperativity of globular proteins structure
    • Kuwajima K. The molten globule as a clue for understanding the folding and cooperativity of globular proteins structure. Proteins: Struct. Funct. Genet. 6:1989;87-103
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 36
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh S.N., Kay M.S., Baldwin R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Nat. Acad. Sci. USA. 92:1995;5446-5450
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 37
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton. Oxford, New York, Tokyo: IRL Press at Oxford University Press
    • Pace C.N., Shirley B.A., Thomson J.A. Measuring the conformational stability of a protein. Creighton T.E. Protein Structure. A Practical Approach. 1989;311-330 IRL Press at Oxford University Press, Oxford, New York, Tokyo
    • (1989) Protein Structure. a Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 38
    • 0027322906 scopus 로고
    • Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate
    • Palleros D.R., Shi L., Reid K.L., Fink A.L. Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate. Biochemistry. 32:1993;4314-4321
    • (1993) Biochemistry , vol.32 , pp. 4314-4321
    • Palleros, D.R.1    Shi, L.2    Reid, K.L.3    Fink, A.L.4
  • 39
    • 0015920746 scopus 로고
    • Stages in the mechanism of self-organization of protein molecules
    • Ptitsyn O.B. Stages in the mechanism of self-organization of protein molecules. Dokl. Acad. Nauk SSSR. 210:1973;1213-1215
    • (1973) Dokl. Acad. Nauk SSSR , vol.210 , pp. 1213-1215
    • Ptitsyn, O.B.1
  • 40
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn O.B. Protein folding hypotheses and experiments. J. Protein Chem. 6:1987;273-293
    • (1987) J. Protein Chem. , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 41
    • 0002940127 scopus 로고
    • The molten globule state
    • T.E. Creighton. New York: W. H. Freeman and Company
    • Ptitsyn O.B. The molten globule state. Creighton T.E. Protein Folding. 1992;243-300 W. H. Freeman and Company, New York
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 42
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Advan. Protein Chem. 47:1995;83-229
    • (1995) Advan. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 43
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov P.L. Intermediate states in protein folding. J. Mol. Biol. 258:1996;707-725
    • (1996) J. Mol. Biol. , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 50
    • 0013800421 scopus 로고
    • The interaction of naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites
    • Stryer L. The interaction of naphthalene dye with apomyoglobin and apohemoglobin A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:1965;482-495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 51
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer L. Fluorescence spectroscopy of proteins. Science. 162:1968;526-540
    • (1968) Science , vol.162 , pp. 526-540
    • Stryer, L.1
  • 52
    • 0025911196 scopus 로고
    • Folding of staphylococcal nuclease a studied by equilibrium and kinetic circular dichroism spectra
    • Sugawara T., Kuwajima K., Sugai S. Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. Biochemisty. 30:1991;2698-2706
    • (1991) Biochemisty , vol.30 , pp. 2698-2706
    • Sugawara, T.1    Kuwajima, K.2    Sugai, S.3
  • 53
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;121-282
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 54
    • 0027733616 scopus 로고
    • Use of fast-protein size-exclusion chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky V.N. Use of fast-protein size-exclusion chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry. 32:1993;13288-13298
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 55
    • 0028311781 scopus 로고
    • Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding
    • Uversky V.N. Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding. Int. J. Bio-Chromatog. 1:1994;103-114
    • (1994) Int. J. Bio-Chromatog. , vol.1 , pp. 103-114
    • Uversky, V.N.1
  • 56
    • 0028176911 scopus 로고
    • "partly folded" state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of β-lactamase at low temperatures
    • Uversky V.N., Ptitsyn O.B. "Partly folded" state, a new equilibrium state of protein molecules four-state guanidinium chloride-induced unfolding of β-lactamase at low temperatures. Biochemistry. 33:1994;2782-2791
    • (1994) Biochemistry , vol.33 , pp. 2782-2791
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 57
    • 0029924194 scopus 로고    scopus 로고
    • Further evidence on the equilibrium "pre-molten globule state": Four-state GdmCl-induced unfolding of carbonic anhydrase at low temperature
    • Uversky V.N., Ptitsyn O.B. Further evidence on the equilibrium "pre-molten globule state" Four-state GdmCl-induced unfolding of carbonic anhydrase at low temperature. J. Mol. Biol. 255:1996;215-228
    • (1996) J. Mol. Biol. , vol.255 , pp. 215-228
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 58
    • 0040495009 scopus 로고
    • Unfolding of the molten globule state by strong denaturants follows the "all-or-none" principles
    • Uversky V.N., Semisotnov G.V., Ptitsyn O.B. Unfolding of the molten globule state by strong denaturants follows the "all-or-none" principles. Biophysics (Moscow). 38:1993;31-39
    • (1993) Biophysics (Moscow) , vol.38 , pp. 31-39
    • Uversky, V.N.1    Semisotnov, G.V.2    Ptitsyn, O.B.3
  • 60
    • 0031010618 scopus 로고    scopus 로고
    • Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
    • Wallenhorst W.F., Green S.M., Roder H. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry. 36:1997;5795-5805
    • (1997) Biochemistry , vol.36 , pp. 5795-5805
    • Wallenhorst, W.F.1    Green, S.M.2    Roder, H.3
  • 61
    • 0030628174 scopus 로고    scopus 로고
    • Residual helical and turn structure in the denatured state of staphylococcal nuclease: Analysis of peptide fragments
    • Wang Y., Shortle D. Residual helical and turn structure in the denatured state of staphylococcal nuclease analysis of peptide fragments. Folding Design. 2:1997;93-100
    • (1997) Folding Design , vol.2 , pp. 93-100
    • Wang, Y.1    Shortle, D.2
  • 62
    • 0030592173 scopus 로고    scopus 로고
    • Sequential unfolding of adenylate kinase during denaturation by guanidine hydrochloride
    • Zhang Y.-L., Zhou J.-M., Tsou C.-L. Sequential unfolding of adenylate kinase during denaturation by guanidine hydrochloride. Biochem. Biophys. Acta. 1295:1996;239-244
    • (1996) Biochem. Biophys. Acta. , vol.1295 , pp. 239-244
    • Zhang, Y.-L.1    Zhou, J.-M.2    Tsou, C.-L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.