메뉴 건너뛰기




Volumn 259, Issue 3, 1996, Pages 512-523

The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence, NMR and small-angle X-ray scattering

Author keywords

Cytochrome c; Helical alcohol denatured state; Methanol induced conformational transition; Molten globule state; Small angle X ray scattering

Indexed keywords

ACID; CYTOCHROME C; METHANOL;

EID: 0029893286     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0336     Document Type: Article
Times cited : (170)

References (61)
  • 1
    • 0028009873 scopus 로고
    • Characterization of a trifluoroethanol-induced partially folded state of α-lactalbumin
    • Alexandrescu, A. T., Ng, Y. L. & Dobson, C. M. (1994). Characterization of a trifluoroethanol-induced partially folded state of α-lactalbumin. J. Mol. Biol. 235, 587-599.
    • (1994) J. Mol. Biol. , vol.235 , pp. 587-599
    • Alexandrescu, A.T.1    Ng, Y.L.2    Dobson, C.M.3
  • 2
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochrome c
    • Babul, J. & Stellwagen, E. (1972). Participation of the protein ligands in the folding of cytochrome c. Biochemistry, 11, 1195-1120.
    • (1972) Biochemistry , vol.11 , pp. 1195-11120
    • Babul, J.1    Stellwagen, E.2
  • 3
    • 0027254057 scopus 로고
    • The molten globule intermediate of apomyoglobin and the process of protein folding
    • Barrick, D. & Baldwin, R. L. (1993a). The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2, 869-876.
    • (1993) Protein Sci. , vol.2 , pp. 869-876
    • Barrick, D.1    Baldwin, R.L.2
  • 4
    • 0027245421 scopus 로고
    • The three-state analysis of sperm whale apomyoglobin folding
    • Barrick, D. & Baldwin, R. L. (1993b). The three-state analysis of sperm whale apomyoglobin folding. Biochemistry, 32, 3790-3796.
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 5
    • 0014939906 scopus 로고
    • The role of aliphatic alcohols on the stability of collagen and tropocollagen
    • Bianchi, E., Rampone, R., Tealdi, A. & Ciferri, A. (1970). The role of aliphatic alcohols on the stability of collagen and tropocollagen. J. Biol. Chem. 245, 3341-3345.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3341-3345
    • Bianchi, E.1    Rampone, R.2    Tealdi, A.3    Ciferri, A.4
  • 6
    • 0027492170 scopus 로고
    • A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implications for protein folding
    • Buck, M., Radford, S. E. & Dobson, C. M. (1993). A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Biochemistry, 32, 667-678.
    • (1993) Biochemistry , vol.32 , pp. 667-678
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 7
    • 0028882136 scopus 로고
    • Characterization of conformational preferences in a partially folded protein by heteronuclear NMR spectroscopy: Assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol
    • Buck, M., Schwalbe, H. & Dobson, C. M. (1995). Characterization of conformational preferences in a partially folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol. Biochemistry, 34, 13219-13232.
    • (1995) Biochemistry , vol.34 , pp. 13219-13232
    • Buck, M.1    Schwalbe, H.2    Dobson, C.M.3
  • 8
    • 0014939887 scopus 로고
    • The effect of aliphatic alcohols on the helix-coil transition of poly-1-ornithine and poly-1-glutamic acid
    • Conio, G., Patrone, E. & Brighetti, S. (1970). The effect of aliphatic alcohols on the helix-coil transition of poly-1-ornithine and poly-1-glutamic acid. J. Biol. Chem. 245, 3335-3340.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3335-3340
    • Conio, G.1    Patrone, E.2    Brighetti, S.3
  • 9
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton, T. E. (1990). Protein folding. Biochem. J. 270, 1-15.
    • (1990) Biochem. J. , vol.270 , pp. 1-15
    • Creighton, T.E.1
  • 10
    • 0025732606 scopus 로고
    • Acid denatured apo-cytochrome c is a random coil: Evidence from small-angle X-ray scattering and dynamic light scattering
    • Damaschun, G., Damaschun, H., Gast, K., Gernat, C. & Zirwer, D. (1991). Acid denatured apo-cytochrome c is a random coil: evidence from small-angle X-ray scattering and dynamic light scattering. Biochim. Biophys. Acta, 1078, 289-295.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 289-295
    • Damaschun, G.1    Damaschun, H.2    Gast, K.3    Gernat, C.4    Zirwer, D.5
  • 12
    • 0027155642 scopus 로고
    • Redesign of the interior hydrophobic region of mitochondrial cytochrome c by site-directed mutagenesis
    • Davies, A. M., Guillemette, J. G., Smith, M., Greenwood, C., Thurgood, A. G. P., Mauk, A. G. & Moore, G. R. (1993). Redesign of the interior hydrophobic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry, 32, 5431-5435.
    • (1993) Biochemistry , vol.32 , pp. 5431-5435
    • Davies, A.M.1    Guillemette, J.G.2    Smith, M.3    Greenwood, C.4    Thurgood, A.G.P.5    Mauk, A.G.6    Moore, G.R.7
  • 13
    • 0001877468 scopus 로고
    • Characterization of protein folding intermediate
    • Dobson, C. M. (1991). Characterization of protein folding intermediate. Curr. Opin. Struct. Biol. 1, 22-27.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 22-27
    • Dobson, C.M.1
  • 14
    • 0001931668 scopus 로고
    • Unfolded proteins, compact states and molten globules
    • Dobson, C. M. (1992). Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2, 6-12.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 6-12
    • Dobson, C.M.1
  • 15
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
    • Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A. & Wright, P. E. (1992a). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226, 795-817.
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 16
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Plastocyanin
    • Dyson, H. J., Sayre, J. R., Merutka, G., Shin, H. C., Lerner, R. A. & Wright, P. E. (1992b). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Plastocyanin. J. Mol. Biol. 226, 819-835.
    • (1992) J. Mol. Biol. , vol.226 , pp. 819-835
    • Dyson, H.J.1    Sayre, J.R.2    Merutka, G.3    Shin, H.C.4    Lerner, R.A.5    Wright, P.E.6
  • 17
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve, G. A., Bhuyan, A. K. & Roder, H. (1994). Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands. Biochemistry, 33, 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 18
    • 0027526627 scopus 로고
    • Structural characterization of monellin in the alcohol-denatured state by NMR: Evidence for β-sheet to α-helix conversion
    • Fan, P., Bracken, C. & Baum, J. (1993). Structural characterization of monellin in the alcohol-denatured state by NMR: evidence for β-sheet to α-helix conversion. Biochemistry, 32, 1573-1583.
    • (1993) Biochemistry , vol.32 , pp. 1573-1583
    • Fan, P.1    Bracken, C.2    Baum, J.3
  • 19
    • 0023118118 scopus 로고
    • Characterization of the unfolding of ribonuclease A in aqueous methanol solvent
    • Fink, A. L. & Painter, B. (1987). Characterization of the unfolding of ribonuclease A in aqueous methanol solvent. Biochemistry, 26, 1665-1671.
    • (1987) Biochemistry , vol.26 , pp. 1665-1671
    • Fink, A.L.1    Painter, B.2
  • 21
    • 0027495402 scopus 로고
    • Mutation can cause large changes in the conformation of a denatured protein
    • Flanagan, J. M., Kataoka, M., Fujisawa, T. & Engelman, D. M. (1993). Mutation can cause large changes in the conformation of a denatured protein. Biochemistry, 32, 10359-10370.
    • (1993) Biochemistry , vol.32 , pp. 10359-10370
    • Flanagan, J.M.1    Kataoka, M.2    Fujisawa, T.3    Engelman, D.M.4
  • 23
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acid molten globule of cytochrome c
    • Goto, Y. & Nishikiori, S. (1991). Role of electrostatic repulsion in the acid molten globule of cytochrome c. J. Mol. Biol. 222, 679-686.
    • (1991) J. Mol. Biol. , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikiori, S.2
  • 25
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., Takahashi, N. & Fink, A. L. (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
  • 28
    • 0027323022 scopus 로고
    • Guanidine hydrochloride-induced folding of proteins
    • Hagihara, Y., Aimoto, S., Fink, A. L. & Goto, Y. (1993). Guanidine hydrochloride-induced folding of proteins. J. Mol. Biol. 231, 180-184.
    • (1993) J. Mol. Biol. , vol.231 , pp. 180-184
    • Hagihara, Y.1    Aimoto, S.2    Fink, A.L.3    Goto, Y.4
  • 29
    • 0025731274 scopus 로고
    • Characterization of a partially denatured state of a protein by two-dimensional NMR: Reduction of the hydrophobic interactions in ubiquitin
    • Harding, M. M., Williams, D. H. & Woolfson, D. N. (1991). Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin. Biochemistry, 30, 3120-3128.
    • (1991) Biochemistry , vol.30 , pp. 3120-3128
    • Harding, M.M.1    Williams, D.H.2    Woolfson, D.N.3
  • 30
    • 0014962109 scopus 로고
    • On the structural stability and solvent denaturation of proteins
    • Herskovits, T. T., Gadegbeku, B. & Jaillet, H. (1970). On the structural stability and solvent denaturation of proteins. J. Biol. Chem. 245, 2588-2598.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2588-2598
    • Herskovits, T.T.1    Gadegbeku, B.2    Jaillet, H.3
  • 31
    • 0026009213 scopus 로고
    • Stable submolecular folding units in non-compact form of cytochrome c
    • Jeng, M. F. & Englander, S. W. (1991). Stable submolecular folding units in non-compact form of cytochrome c. J. Mol. Biol. 221, 1045-1061.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1045-1061
    • Jeng, M.F.1    Englander, S.W.2
  • 32
    • 0025203243 scopus 로고
    • Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
    • Jeng, M. F., Englander, S. W., Elöve, G. A., Wand, A. J. & Roder, H. (1990). Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry, 29, 10433-10437.
    • (1990) Biochemistry , vol.29 , pp. 10433-10437
    • Jeng, M.F.1    Englander, S.W.2    Elöve, G.A.3    Wand, A.J.4    Roder, H.5
  • 33
    • 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. (1989). Melittin binding causes a large calcium-dependent conformational change in calmodulin. Proc. Natl Acad. Sci. USA, 86, 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
  • 34
    • 0025778565 scopus 로고
    • Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly α-helical conformation
    • Kataoka, M., Head, J. F., Persechini, A., Kretsinger, R. H. & Engelman, D. M. (1991). Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly α-helical conformation. Biochemistry, 30, 1188-1192.
    • (1991) Biochemistry , vol.30 , pp. 1188-1192
    • Kataoka, M.1    Head, J.F.2    Persechini, A.3    Kretsinger, R.H.4    Engelman, D.M.5
  • 35
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by the small angle X-ray scattering
    • Kataoka, M., Hagihara, Y., Mihara, K. & Goto, Y. (1993). Molten globule of cytochrome c studied by the 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
  • 36
    • 0001885952 scopus 로고
    • Use of X-ray solution scattering for protein folding study
    • (Chance, B., Deisenhofer, J., Ebashi, S., Goodhead, D. T., Helliwell, J. R., Huxley H. E., lizuka, T., Kirz, J., Mitsui, T., Rubenstein, E., Sakabe, N., Sasaki, T., Schmahl, G., Stuhrmann, H. B., Wüthrich, K. & Zaccai, G., eds), Clarendon Press, Oxford
    • Kataoka, M., Flanagan, J. M., Tokunaga, F. & Engelman, D. M. (1994). Use of X-ray solution scattering for protein folding study In Synchrotron Radiation in the Biosciences (Chance, B., Deisenhofer, J., Ebashi, S., Goodhead, D. T., Helliwell, J. R., Huxley H. E., lizuka, T., Kirz, J., Mitsui, T., Rubenstein, E., Sakabe, N., Sasaki, T., Schmahl, G., Stuhrmann, H. B., Wüthrich, K. & Zaccai, G., eds), pp. 187-194, Clarendon Press, Oxford.
    • (1994) Synchrotron Radiation in the Biosciences , pp. 187-194
    • Kataoka, M.1    Flanagan, J.M.2    Tokunaga, F.3    Engelman, D.M.4
  • 37
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F. & Goto, T. (1995). Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249, 215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, T.6
  • 38
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S. & Baldwin, R. L. (1990). Intermediates in the folding reactions of small proteins. Annn. Rev. Biochem. 59, 946-950.
    • (1990) Annn. Rev. Biochem. , vol.59 , pp. 946-950
    • Kim, P.S.1    Baldwin, R.L.2
  • 40
    • 0029126840 scopus 로고
    • Solution X-ray scattering analysis of cold-, heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor
    • Konno, T., Kataoka, M., Kamatari, Y., Kanaori, K., Nosaka, A. & Akasaka, K. (1995). Solution X-ray scattering analysis of cold-, heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor. J. Mol. Biol. 251, 95-103.
    • (1995) J. Mol. Biol. , vol.251 , pp. 95-103
    • Konno, T.1    Kataoka, M.2    Kamatari, Y.3    Kanaori, K.4    Nosaka, A.5    Akasaka, K.6
  • 41
    • 0026525049 scopus 로고
    • Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process
    • Kuroda, Y., Kidokoro, S. & Wada, A. (1992). Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process. J. Mol. Biol. 223, 1139-1153.
    • (1992) J. Mol. Biol. , vol.223 , pp. 1139-1153
    • Kuroda, Y.1    Kidokoro, S.2    Wada, A.3
  • 42
    • 0028988453 scopus 로고
    • Stability of α-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy
    • Kuroda, Y., Endo, S., Nagayama, K. & Wada, A. (1995). Stability of α-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy J. Mol. Biol. 247, 682-688.
    • (1995) J. Mol. Biol. , vol.247 , pp. 682-688
    • Kuroda, Y.1    Endo, S.2    Nagayama, K.3    Wada, A.4
  • 43
    • 0024417964 scopus 로고
    • The molten globule states as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989). The molten globule states as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6, 87-103.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 44
    • 0026940839 scopus 로고
    • Protein folding in vivo
    • Kuwajima, K. (1992). Protein folding in vivo. Curr. Opin. Biotechnol. 3, 462-467.
    • (1992) Curr. Opin. Biotechnol. , vol.3 , pp. 462-467
    • Kuwajima, K.1
  • 45
    • 0027955639 scopus 로고
    • Small angle scattering studies of protein folding
    • Lattman, E. E. (1994). Small angle scattering studies of protein folding. Curr. Opin. Struct. Biol. 4, 87-92.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 87-92
    • Lattman, E.E.1
  • 46
    • 0025300073 scopus 로고
    • Peptide α-helicity in aqueous trifluoroethanol: Correlations with predicted α-helicity and the secondary structure of the corresponding regions of bovine growth hormone
    • Lehrman, S. R., Tuls, J. L. & Lund, M. (1990). Peptide α-helicity in aqueous trifluoroethanol: correlations with predicted α-helicity and the secondary structure of the corresponding regions of bovine growth hormone. Biochemistry, 29, 5590-5596.
    • (1990) Biochemistry , vol.29 , pp. 5590-5596
    • Lehrman, S.R.1    Tuls, J.L.2    Lund, M.3
  • 47
    • 0025325351 scopus 로고
    • The folding of staphylococcal nuclease in the presence of methanol or guanidine thiocyanate
    • Nakano, T. & Fink, A. L. (1990). The folding of staphylococcal nuclease in the presence of methanol or guanidine thiocyanate. J. Biol. Chem. 265, 12356-12362.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12356-12362
    • Nakano, T.1    Fink, A.L.2
  • 48
    • 0022804939 scopus 로고
    • Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol
    • Nelson, J. W. & Kallenbach, N. R. (1986). Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol. Proteins: Struct. Funct. Genet. 1, 211-217.
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 211-217
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 49
    • 0024473893 scopus 로고
    • Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol
    • Nelson, J. W. & Kallenbach, N. R. (1989). Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol. Biochemistry, 28, 5256-5261.
    • (1989) Biochemistry , vol.28 , pp. 5256-5261
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 50
    • 0028243107 scopus 로고
    • Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii, I., Kataoka, M., Tokunaga, F. & Goto, Y. (1994). Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry, 33, 4903-4909.
    • (1994) Biochemistry , vol.33 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 51
    • 0021114569 scopus 로고
    • "Molten-globule state": A compact form of globular proteins with mobile side-chains
    • Ohgushi, M. & Wada, A. (1983). "Molten-globule state": a compact form of globular proteins with mobile side-chains. FEBS Letters, 164, 21-24.
    • (1983) FEBS Letters , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 52
    • 0027171026 scopus 로고
    • Leucine/isoleucine/valine binding protein contracts upon binding of ligand
    • Olah, G. A., Trakhanov, S., Trewhella, J. & Quiocho, F. A. (1993). Leucine/isoleucine/valine binding protein contracts upon binding of ligand. J. Biol. Chem. 268, 16241-16247.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16241-16247
    • Olah, G.A.1    Trakhanov, S.2    Trewhella, J.3    Quiocho, F.A.4
  • 53
    • 0002940127 scopus 로고
    • The molten globule state
    • (Creighton, T. E., ed.), W. H. Freeman and Company New York
    • Ptitsyn, O. B. (1992). The molten globule state. In Protein Folding (Creighton, T. E., ed.), pp. 243-300, W. H. Freeman and Company New York.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 54
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn, O. B. (1995). Structures of folding intermediates. Curr. Opin. Struct. Biol. 5, 74-78.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 55
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder, H., Elöve, G. A. & Englander, S. W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature, 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 56
    • 0026143167 scopus 로고
    • Local structure in unfolded lysozyme and correlation with secondary structures in the native conformation: Helix-forming or -breaking propensity of peptide segments
    • Segawa, S., Fukuno, T., Fujiwara, K. & Noda, Y. (1991). Local structure in unfolded lysozyme and correlation with secondary structures in the native conformation: helix-forming or -breaking propensity of peptide segments. Biopolymers, 31, 497-509.
    • (1991) Biopolymers , vol.31 , pp. 497-509
    • Segawa, S.1    Fukuno, T.2    Fujiwara, K.3    Noda, Y.4
  • 57
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Siraki, K., Nishikawa, K. & Goto, Y. (1995). Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194.
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Siraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 59
    • 0022160183 scopus 로고
    • Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation
    • Ueki, T., Hiragi, Y., Kataoka, M., Inoko, Y., Amemiya, Y., Izumi, Y., Tagawa, H. & Muraga, Y. (1985). Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation. Biophys. Chem. 23, 115-124.
    • (1985) Biophys. Chem. , vol.23 , pp. 115-124
    • Ueki, T.1    Hiragi, Y.2    Kataoka, M.3    Inoko, Y.4    Amemiya, Y.5    Izumi, Y.6    Tagawa, H.7    Muraga, Y.8
  • 61
    • 0027442944 scopus 로고
    • A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c
    • Wu, L. C., Laub, P B., Elöve, G. A., Carey J. & Roder, H. (1993). A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry, 32, 10271-10276.
    • (1993) Biochemistry , vol.32 , pp. 10271-10276
    • Wu, L.C.1    Laub, P.B.2    Elöve, G.A.3    Carey, J.4    Roder, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.