메뉴 건너뛰기




Volumn 8, Issue 1, 1999, Pages 161-173

Association of partially-folded intermediates of staphylococcal nuclease induces structure and stability

Author keywords

Aggregation; Anion induced protein folding; Conformational phase diagram; Small angle X ray scattering

Indexed keywords

ANION; BACTERIAL ENZYME; DIMER; MONOMER; NUCLEASE; OLIGOMER;

EID: 0032932954     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.1.161     Document Type: Article
Times cited : (66)

References (50)
  • 1
    • 0014730026 scopus 로고
    • Analytical gel chromatography of proteins
    • Ackers GK. 1970. Analytical gel chromatography of proteins. Adv Protein Chem 24:343-446.
    • (1970) Adv Protein Chem , vol.24 , pp. 343-446
    • Ackers, G.K.1
  • 2
    • 0015240523 scopus 로고
    • The specific binding of three fragments of staphylococcal nuclease
    • Andria G, Taniuchi H, Cone JL. 1971. The specific binding of three fragments of staphylococcal nuclease. J Biol Chem 246:7421-7428.
    • (1971) J Biol Chem , vol.246 , pp. 7421-7428
    • Andria, G.1    Taniuchi, H.2    Cone, J.L.3
  • 3
    • 0028865843 scopus 로고
    • 3D domain swapping a mechanism for oligomer assembly
    • Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
    • (1995) Protein Sci , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 4
    • 0023039205 scopus 로고
    • Characterization of an associated equilibrium folding intermediate of bovine growth hormone
    • Brems DN, Plaisted SM, Kauffman EW, Havel HA. 1986. Characterization of an associated equilibrium folding intermediate of bovine growth hormone. Biochemistry 25:6539-6543.
    • (1986) Biochemistry , vol.25 , pp. 6539-6543
    • Brems, D.N.1    Plaisted, S.M.2    Kauffman, E.W.3    Havel, H.A.4
  • 5
    • 0019536747 scopus 로고
    • Infrared and laser-raman spectroscopic studies of thermally-induced globular protein gels
    • Clark AH, Saunderson DH, Suggett A. 1981. Infrared and laser-raman spectroscopic studies of thermally-induced globular protein gels. Int J Peptide Protein Res 17:353-364.
    • (1981) Int J Peptide Protein Res , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.2    Suggett, A.3
  • 6
    • 0021759423 scopus 로고
    • Use of high-speed size-exclusion chromatography for the study of proteins
    • Corbett RJ, Roche RS. 1984. Use of high-speed size-exclusion chromatography for the study of proteins. Biochemistry 23:1888-1894.
    • (1984) Biochemistry , vol.23 , pp. 1888-1894
    • Corbett, R.J.1    Roche, R.S.2
  • 7
    • 0027502115 scopus 로고
    • Evidence for a self-associating equilibrium intermediate during folding of human growth hormone
    • Defelippis MR, Alter LA, Pekar AH, Havel HA, Brems DN. 1993. Evidence for a self-associating equilibrium intermediate during folding of human growth hormone. Biochemistry 52:1555-1562.
    • (1993) Biochemistry , vol.52 , pp. 1555-1562
    • Defelippis, M.R.1    Alter, L.A.2    Pekar, A.H.3    Havel, H.A.4    Brems, D.N.5
  • 11
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink AL. 1995. Compact intermediate states in protein folding. Ann Rev Biophys Biomol Struct 24:495-522.
    • (1995) Ann Rev Biophys Biomol Struct , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 12
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Design 3:R9-15.
    • (1998) Fold Design , vol.3
    • Fink, A.L.1
  • 13
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. 1994. Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry 33:12504-12511.
    • (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
  • 14
    • 0027241814 scopus 로고
    • Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
    • Fink AL, Calciano LJ, Goto Y, Nishimura M, Swedberg SA. 1993. Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Sci 2:1155-1160.
    • (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
  • 15
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates vs. Molten globule models of protein folding: Characterization of partially-folded intermediates of apomyoglobin
    • Fink AL, Oberg KA, Seshadri S. 1997. Discrete intermediates vs. molten globule models of protein folding: Characterization of partially-folded intermediates of apomyoglobin. Fold Design 3:19-25.
    • (1997) Fold Design , vol.3 , pp. 19-25
    • Fink, A.L.1    Oberg, K.A.2    Seshadri, S.3
  • 16
    • 0028559525 scopus 로고
    • Folding and aggregation of TEM β-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli
    • Georgiou G, Valax P, Ostermeier M, Horowitz PM. 1994. Folding and aggregation of TEM β-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli. Protein Sci 3:1953-1960.
    • (1994) Protein Sci , vol.3 , pp. 1953-1960
    • Georgiou, G.1    Valax, P.2    Ostermeier, M.3    Horowitz, P.M.4
  • 19
    • 0024963570 scopus 로고
    • Conformational states of beta-lactamase: Molten-globule states at acidic and alkaline pH with high salt
    • Goto Y, Fink AL. 1989. Conformational states of beta-lactamase: Molten-globule states at acidic and alkaline pH with high salt. Biochemistry 28:945-952.
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 20
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y, Takahashi N, Fink AL. 1990b. Mechanism of acid-induced folding of proteins. Biochemistry 29:3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 22
    • 0022976484 scopus 로고
    • Reversible self-association of bovine growth hormone during equilibrium unfolding
    • Havel HA, Kauffman EW, Plaisted SM, Brems DN. 1986. Reversible self-association of bovine growth hormone during equilibrium unfolding. Biochemistry 25:6533-6538.
    • (1986) Biochemistry , vol.25 , pp. 6533-6538
    • Havel, H.A.1    Kauffman, E.W.2    Plaisted, S.M.3    Brems, D.N.4
  • 23
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by small angle X-ray scattering
    • Kataoka M, Hagihara Y, Mihara K, Goto Y. 1993. Molten globule of cytochrome c studied by small angle X-ray scattering. J Mol Biol 229:591-596.
    • (1993) J Mol Biol , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 24
    • 0016206102 scopus 로고
    • Renaturation of Escherichia coli tryptophanase after exposure to 8 m urea. Evidence for the existence of nucleation centers
    • London J, Skrzynia C, Goldberg ME. 1974. Renaturation of Escherichia coli tryptophanase after exposure to 8 m urea. Evidence for the existence of nucleation centers. Eur J Biochem 47:409-415.
    • (1974) Eur J Biochem , vol.47 , pp. 409-415
    • London, J.1    Skrzynia, C.2    Goldberg, M.E.3
  • 25
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • Marston FAO. 1986. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem J 240:1-12.
    • (1986) Biochem J , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 26
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki A, King J. 1989. Protein folding intermediates and inclusion body formation. Bio Technology 7:690-697.
    • (1989) Bio Technology , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 27
    • 0028260192 scopus 로고
    • Nativelike secondary structure in interleukin-1-beta inclusion bodies by attenuated total reflectance FT-IR
    • Oberg K, Chrunyk BA, Wetzel R, Fink AL. 1994. Nativelike secondary structure in interleukin-1-beta inclusion bodies by attenuated total reflectance FT-IR. Biochemistry 33:2628-2634.
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 28
    • 0032005382 scopus 로고    scopus 로고
    • A new attenuated total reflectance fourier transform infrared spectroscopy method for the study of proteins in solution
    • Oberg KA, Fink AL. 1998. A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution. Anal Biochem 256:92-106.
    • (1998) Anal Biochem , vol.256 , pp. 92-106
    • Oberg, K.A.1    Fink, A.L.2
  • 29
    • 0019876883 scopus 로고
    • Further study of the conformation of nuclease-(1-126) in relation to intrinsic enzymatic activity
    • Parker DS, Davis A, Taniuchi H. 1981. Further study of the conformation of nuclease-(1-126) in relation to intrinsic enzymatic activity. J Biol Chem 256:4557-4569.
    • (1981) J Biol Chem , vol.256 , pp. 4557-4569
    • Parker, D.S.1    Davis, A.2    Taniuchi, H.3
  • 30
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. 1995. Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 32
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein CH. 1989. Production of soluble recombinant proteins in bacteria. Bio Technology 7:1141-1149.
    • (1989) Bio Technology , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 36
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow M, Oliveberg M. 1997. Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc Natl Acad Sci USA 94:6084-6086.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 37
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe for nonpolar sites
    • Stryer L. 1965. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe for nonpolar sites. J Mol Biol 13:482-495.
    • (1965) J Mol Biol , vol.13 , pp. 482-495
    • Stryer, L.1
  • 38
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer L. 1968. Fluorescence spectroscopy of proteins. Science 162:526-533.
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 39
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. 1968. Protein denaturation. Adv Protein Chem 23:121-282.
    • (1968) Adv Protein Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 40
    • 0015217635 scopus 로고
    • Simultaneous formation of two alternative enzymology active structures by complementation of two overlapping fragments of staphylococcal nuclease
    • Taniuchi H, Anfinsen CB. 1971. Simultaneous formation of two alternative enzymology active structures by complementation of two overlapping fragments of staphylococcal nuclease. J Biol Chem 246:2291-2301.
    • (1971) J Biol Chem , vol.246 , pp. 2291-2301
    • Taniuchi, H.1    Anfinsen, C.B.2
  • 41
    • 0015523065 scopus 로고
    • A comparison of the X-ray diffraction patterns of crystals of reconstituted nuclease-T and of native staphylococcal nuclease
    • Taniuchi H, Davies DR, Anfinsen CB. 1972. A comparison of the X-ray diffraction patterns of crystals of reconstituted nuclease-T and of native staphylococcal nuclease. J Biol Chem 247:3362-3364.
    • (1972) J Biol Chem , vol.247 , pp. 3362-3364
    • Taniuchi, H.1    Davies, D.R.2    Anfinsen, C.B.3
  • 42
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas PJ, Qu BH, Pedersen PL. 1995. Defective protein folding as a basis of human disease. Trends Biochem Sci 20:456-459.
    • (1995) Trends Biochem Sci , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.H.2    Pedersen, P.L.3
  • 43
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky VN. 1993. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32:13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 44
    • 0028311781 scopus 로고
    • Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding
    • Uversky VN. 1994. Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding. Int J Bio Chem 1:103-114.
    • (1994) Int J Bio Chem , vol.1 , pp. 103-114
    • Uversky, V.N.1
  • 45
    • 0032510674 scopus 로고    scopus 로고
    • Association of partially-folded intermediates of staphylococcal nuclease induces structure and stability
    • Uversky VN, Karnoup AS, Segel DJ, Doniach S, Fink AL. 1998a. Association of partially-folded intermediates of staphylococcal nuclease induces structure and stability. Proc Nat Acad Sci US 95:5480-5483.
    • (1998) Proc Nat Acad Sci US , vol.95 , pp. 5480-5483
    • Uversky, V.N.1    Karnoup, A.S.2    Segel, D.J.3    Doniach, S.4    Fink, A.L.5
  • 46
    • 0032525256 scopus 로고    scopus 로고
    • Anion-induced folding of staphylococcal nuclease: Characterization of multiple equilibrium folding intermediates
    • Uversky VN, Karnoup AS, Segel DJ, Seshadri S, Doniach S, Fink AL. 1998b. Anion-induced folding of staphylococcal nuclease: Characterization of multiple equilibrium folding intermediates. J Mol Biol 278:879-894.
    • (1998) J Mol Biol , vol.278 , pp. 879-894
    • Uversky, V.N.1    Karnoup, A.S.2    Segel, D.J.3    Seshadri, S.4    Doniach, S.5    Fink, A.L.6
  • 47
    • 0028176911 scopus 로고
    • "Partly folded" state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature
    • Uversky VN, Ptitsyn OB. 1994. "Partly folded" state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. Biochemistry 33:2782-2791.
    • (1994) Biochemistry , vol.33 , pp. 2782-2791
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 48
    • 0029924194 scopus 로고    scopus 로고
    • Further evidence on the equilibrium "pre-molten globule state": Four-state guanidinium chloride-induced unfolding of carbonic anhydrase b at low temperature
    • Uversky VN, Ptitsyn OB. 1996. Further evidence on the equilibrium "pre-molten globule state": Four-state guanidinium chloride-induced unfolding of carbonic anhydrase b at low temperature. J Mol Biol 255:215-228.
    • (1996) J Mol Biol , vol.255 , pp. 215-228
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 50
    • 0001282018 scopus 로고
    • Principles of protein stability. Part 2: Enhanced folding and stabilization of proteins by suppression of aggregation in vitro and in vivo
    • Rees AR, Stemberg MJE, eds. Oxford: Irl Press at Oxford University Press
    • Wetzel R. 1992b. Principles of protein stability. Part 2: Enhanced folding and stabilization of proteins by suppression of aggregation in vitro and in vivo. In: Rees AR, Stemberg MJE, eds. Protein engineering: A practical approach. Oxford: IRL Press at Oxford University Press. pp 191-219.
    • (1992) Protein Engineering: A Practical Approach , pp. 191-219
    • Wetzel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.