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Volumn 275, Issue 2, 1998, Pages 379-388

Native tertiary structure in an A-state

Author keywords

Circular dichroism; Cytochrome c; Molten globule; Protein folding; Protein stability

Indexed keywords

CYTOCHROME C; SULFATE;

EID: 0032536105     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1450     Document Type: Article
Times cited : (74)

References (52)
  • 1
    • 0025953443 scopus 로고
    • Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis
    • Auld, D. S. & Pielak, G. J. (1991). Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis. Biochemistry, 30, 8684-8690.
    • (1991) Biochemistry , vol.30 , pp. 8684-8690
    • Auld, D.S.1    Pielak, G.J.2
  • 2
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R. L. (1996). On-pathway versus off-pathway folding intermediates. Fold. Des. 1, R1-R8.
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 4
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. J. & Schellman, J. A. (1987). Protein stability curves. Biopolymers, 26, 1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 5
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis, A. M. & Brayer, G. D. (1992). Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223, 959-976.
    • (1992) J. Mol. Biol. , vol.223 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 6
    • 0027000943 scopus 로고
    • Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state
    • Betz, S. F. & Pielak, G. J. (1992). Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state. Biochemistry, 31, 12337-12344.
    • (1992) Biochemistry , vol.31 , pp. 12337-12344
    • Betz, S.F.1    Pielak, G.J.2
  • 7
    • 0000837519 scopus 로고    scopus 로고
    • Structural studies of eukaryotic cytochromes c
    • (Scott, R. A. & Mauk, A. G., eds), University Science Books, Sausalito
    • Brayer, G. D. & Murphy, M. E. P. (1996). Structural studies of eukaryotic cytochromes c. In Cytochrome c: A Multidisciplinary Approach. (Scott, R. A. & Mauk, A. G., eds), pp. 103-166, University Science Books, Sausalito.
    • (1996) Cytochrome C: A Multidisciplinary Approach , pp. 103-166
    • Brayer, G.D.1    Murphy, M.E.P.2
  • 8
    • 0027935843 scopus 로고
    • Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature
    • Cohen, D. S. & Pielak, G. J. (1994). Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature. Protein Sci. 3, 1253-1260.
    • (1994) Protein Sci. , vol.3 , pp. 1253-1260
    • Cohen, D.S.1    Pielak, G.J.2
  • 9
    • 0028847055 scopus 로고
    • Entropic stabilization of cytochrome c upon reduction
    • Cohen, D. S. & Pielak, G. J. (1995). Entropic stabilization of cytochrome c upon reduction. J. Am. Chem. Soc. 117, 1675-1677.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1675-1677
    • Cohen, D.S.1    Pielak, G.J.2
  • 10
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Colón, W. & Roder, H. (1996). Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Struct. Biol. 3, 1019-1025.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1019-1025
    • Colón, W.1    Roder, H.2
  • 11
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N- And C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colón, W., Elöve, G. A., Wakem, L. P., Sherman, F. & Roder, H. (1996). Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry, 35, 5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colón, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 13
    • 0023290578 scopus 로고
    • Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: Improved stability of the mutant protein
    • Cutler, R. L., Pielak, G. J., Mauk, A. G. & Smith, M. (1987). Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Eng. 1, 95-99.
    • (1987) Protein Eng. , vol.1 , pp. 95-99
    • Cutler, R.L.1    Pielak, G.J.2    Mauk, A.G.3    Smith, M.4
  • 14
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower, W. J., Miller, J. F. & Ragsdale, C. W. (1988). High efficiency transformation of E. coli by high voltage electroporation. Nucl. Acids Res. 16, 6127-6145.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 15
    • 0017718187 scopus 로고
    • Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes
    • Elwell, M. L. & Schellman, J. A. (1977). Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. Biochim. Biophys. Acta, 494, 367-383.
    • (1977) Biochim. Biophys. Acta , vol.494 , pp. 367-383
    • Elwell, M.L.1    Schellman, J.A.2
  • 16
    • 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. (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
  • 18
    • 0027450286 scopus 로고
    • Exploring the interface between the N- And C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix
    • Fredericks, Z. L. & Pielak, G. J. (1993). Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix. Biochemistry, 32, 929-936.
    • (1993) Biochemistry , vol.32 , pp. 929-936
    • Fredericks, Z.L.1    Pielak, G.J.2
  • 19
    • 0025727988 scopus 로고
    • Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts
    • Gao, Y., Boyd, J., Pielak, G. J. & Williams, R. J. P. (1991). Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts. Biochemistry, 30, 1928-1934.
    • (1991) Biochemistry , vol.30 , pp. 1928-1934
    • Gao, Y.1    Boyd, J.2    Pielak, G.J.3    Williams, R.J.P.4
  • 20
    • 0028900809 scopus 로고
    • Protein structure refinement based on paramagnetic NMR shifts: Application to wild-type and mutant forms of cytochrome c
    • Gochin, M. & Roder, H. (1995). Protein structure refinement based on paramagnetic NMR shifts: application to wild-type and mutant forms of cytochrome c. Protein Sci. 4, 296-305.
    • (1995) Protein Sci. , vol.4 , pp. 296-305
    • Gochin, M.1    Roder, H.2
  • 21
    • 0028143596 scopus 로고
    • Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
    • Hamada, D., Kidokoro, S.-I., Fukada, H., Takahashi, K. & Goto, G. (1994). Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl Acad. Sci. USA, 91, 10325-10329.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10325-10329
    • Hamada, D.1    Kidokoro, S.-I.2    Fukada, H.3    Takahashi, K.4    Goto, G.5
  • 22
    • 0029863253 scopus 로고    scopus 로고
    • Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c
    • Hamada, D., Kuroda, Y., Kataoka, M., Aimoto, S., Yoshimura, T. & Goto, Y. (1996). Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J. Mol. Biol. 256, 172-186.
    • (1996) J. Mol. Biol. , vol.256 , pp. 172-186
    • Hamada, D.1    Kuroda, Y.2    Kataoka, M.3    Aimoto, S.4    Yoshimura, T.5    Goto, Y.6
  • 23
    • 0020959710 scopus 로고
    • Studies of transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies of transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 24
    • 0025800137 scopus 로고
    • The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector
    • Hilgen, S. E. & Pielak, G. J. (1991). The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector. Protein Eng. 4, 575-578.
    • (1991) Protein Eng. , vol.4 , pp. 575-578
    • Hilgen, S.E.1    Pielak, G.J.2
  • 26
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A. & Wright, P. E. (1993). Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science, 262, 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 27
    • 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
  • 28
    • 0029981924 scopus 로고    scopus 로고
    • Packing interactions in the apomyoglobin folding intermediate
    • Kay, M. S. & Baldwin, R. L. (1996). Packing interactions in the apomyoglobin folding intermediate. Nature Struct. Biol. 3, 439-445.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 439-445
    • Kay, M.S.1    Baldwin, R.L.2
  • 29
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I. D. & Roder, H (1996). Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3, 193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 30
    • 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.-I. & 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.-I.2    Wada, A.3
  • 32
    • 0028926855 scopus 로고
    • A native tertiary interaction stabilizes the A-state of cytochrome c
    • Marmorino, J. L. & Pielak, G. J. (1995). A native tertiary interaction stabilizes the A-state of cytochrome c. Biochemistry, 34, 3140-3143.
    • (1995) Biochemistry , vol.34 , pp. 3140-3143
    • Marmorino, J.L.1    Pielak, G.J.2
  • 33
    • 0021902977 scopus 로고
    • The structure, function and evolution of cytochromes
    • Matthews, F. S. (1985). The structure, function and evolution of cytochromes. Prog. Biophys. Mol. Biol. 45, 1-56.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 1-56
    • Matthews, F.S.1
  • 36
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: Comparison with experimental scales
    • Muñoz, V. & Serrano, L. (1994). Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: comparison with experimental scales. Proteins: Struct. Funct. Genet. 20, 301-311.
    • (1994) Proteins: Struct. Funct. Genet. , vol.20 , pp. 301-311
    • Muñoz, V.1    Serrano, L.2
  • 37
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N & Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 38
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers, J. K., Pace, C. N. & Scholtz, J. M. (1997). A direct comparison of helix propensity in proteins and peptides. Proc. Natl Acad. Sci. USA. 94, 2833-2837.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 39
    • 0000181415 scopus 로고
    • The influence of amino acid side chains on the free energy of helix-coil transitions
    • Némethy, G., Leach, S. J. & Scheraga, H. A. (1966). The influence of amino acid side chains on the free energy of helix-coil transitions. J. Phys. Chem. 70, 998-1004.
    • (1966) J. Phys. Chem. , vol.70 , pp. 998-1004
    • Némethy, G.1    Leach, S.J.2    Scheraga, H.A.3
  • 40
    • 0024002575 scopus 로고
    • A rapid droplet method for Sanger dideoxy sequencing
    • Ner, S. S., Goodin, D. B., Pielak, G. J. & Smith, M. (1988). A rapid droplet method for Sanger dideoxy sequencing. Biotechniques, 6, 408-412.
    • (1988) Biotechniques , vol.6 , pp. 408-412
    • Ner, S.S.1    Goodin, D.B.2    Pielak, G.J.3    Smith, M.4
  • 42
    • 0013660457 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of class I cytochromes c
    • (Scott, R. A. & Mauk, A. G., eds), University Science Books, Sausalito
    • Pielak, G. J., Auld, D. S., Betz, S. F., Hilgen-Willis, S. E. & Garcia, L. L. (1996). Nuclear magnetic resonance studies of class I cytochromes c. In Cytochrome c: A Multidisciplinary Approach (Scott, R. A. & Mauk, A. G., eds), pp. 203-284, University Science Books, Sausalito.
    • (1996) Cytochrome C: A Multidisciplinary Approach , pp. 203-284
    • Pielak, G.J.1    Auld, D.S.2    Betz, S.F.3    Hilgen-Willis, S.E.4    Garcia, L.L.5
  • 43
    • 0002940127 scopus 로고
    • The molten globule state
    • (Creighton, T. E., ed.), Freeman, New York
    • Ptitsyn, O. B. (1992). The molten globule state. Protein Folding (Creighton, T. E., ed.), pp. 243-300, Freeman, New York.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 44
    • 0029886627 scopus 로고    scopus 로고
    • How molten is the molten globule?
    • Ptitsyn, O. (1996). How molten is the molten globule? Nature Struct. Biol. 3, 488-490.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 488-490
    • Ptitsyn, O.1
  • 45
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke, T. M. & Marqusee, S. (1997). The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol. 4, 298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 46
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colón, W. (1997). Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 47
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • Roder, H., El(ve, G. A. & Englander, S. W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature, 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elve, G.A.2    Englander, S.W.3
  • 48
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific view of the non-cooperative unfolding of a molten globule
    • Schulman, B. A., Kim, P. S., Dobson, C. M. & Redfield, C. (1997). A residue-specific view of the non-cooperative unfolding of a molten globule. Nature Struct. Biol. 4, 630-634.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 51
    • 0028952169 scopus 로고
    • Bipartite structure of the α-lactalbumin molten globule
    • Wu, L. C., Peng, Z.-y. & Kim, P. S. (1995). Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2, 281-286.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.-Y.2    Kim, P.S.3


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