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Volumn 357, Issue 3, 2006, Pages 1009-1025

Structural characterization of an equilibrium unfolding intermediate in cytochrome c

Author keywords

Denaturation; NMR; Protein folding; Spectroscopy; Stability

Indexed keywords

CYTOCHROME C; GUANIDINE HYDROCHLORIDE; METHIONINE; MUTANT PROTEIN; UREA;

EID: 33644940724     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.01.055     Document Type: Article
Times cited : (80)

References (90)
  • 1
    • 0014364651 scopus 로고
    • Protein denaturation
    • C. Tanford Protein denaturation Advan. Protein Chem. 23 1968 121 282
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 2
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • C.N. Pace The stability of globular proteins CRC Crit. Rev. Biochem. 2 1975 1 43
    • (1975) CRC Crit. Rev. Biochem. , vol.2 , pp. 1-43
    • Pace, C.N.1
  • 4
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • O.B. Ptitsyn 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
  • 5
    • 0029185844 scopus 로고
    • Molten globules
    • B.A. Shirley Humana Press Inc. Totowa, NJ
    • A.L. Fink Molten globules B.A. Shirley Protein Stability and Folding vol. 40 1995 Humana Press Inc. Totowa, NJ 343 361
    • (1995) Protein Stability and Folding , vol.40 , pp. 343-361
    • Fink, A.L.1
  • 6
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • M. Arai, and K. Kuwajima Role of the molten globule state in protein folding Advan. Protein Chem. 53 2000 209 282
    • (2000) Advan. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 7
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • P.L. Privalov 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
  • 10
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • H. Roder, and W. Colón Kinetic role of early intermediates in protein folding Curr. Opin. Struct. Biol. 7 1997 15 28
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 11
    • 0031205431 scopus 로고    scopus 로고
    • Protein folding pathways and intermediates
    • A.R. Clarke, and J.P. Waltho Protein folding pathways and intermediates Curr. Opin. Biotechnol. 8 1997 400 410
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 400-410
    • Clarke, A.R.1    Waltho, J.P.2
  • 12
    • 0034581629 scopus 로고    scopus 로고
    • Barriers in protein folding reactions
    • O. Bilsel, and C.R. Matthews Barriers in protein folding reactions Advan. Protein Chem. 53 2000 153 207
    • (2000) Advan. Protein Chem. , vol.53 , pp. 153-207
    • Bilsel, O.1    Matthews, C.R.2
  • 13
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • I.E. Sanchez, and T. Kiefhaber Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding J. Mol. Biol. 325 2003 367 376
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 14
    • 84889765760 scopus 로고    scopus 로고
    • Early events in protein folding explored by rapid mixing methods
    • J. Buchner T. Kiefhaber Wiley-VCH Weinheim
    • H. Roder, K. Maki, R.F. Latypov, H. Cheng, and M.C.R. Shastry Early events in protein folding explored by rapid mixing methods J. Buchner T. Kiefhaber Protein Folding Handbook 2005 Wiley-VCH Weinheim 491 535 (part I)
    • (2005) Protein Folding Handbook , pp. 491-535
    • Roder, H.1    Maki, K.2    Latypov, R.F.3    Cheng, H.4    Shastry, M.C.R.5
  • 15
    • 0015524145 scopus 로고
    • The conformation of horse heart apocytochrome c
    • E. Stellwagen, R. Rysavy, and G. Babul The conformation of horse heart apocytochrome c J. Biol. Chem. 247 1972 8074 8077
    • (1972) J. Biol. Chem. , vol.247 , pp. 8074-8077
    • Stellwagen, E.1    Rysavy, R.2    Babul, G.3
  • 16
    • 0015918913 scopus 로고
    • Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c
    • A. Ikai, W.W. Fish, and C. Tanford Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c J. Mol. Biol. 73 1973 165 184
    • (1973) J. Mol. Biol. , vol.73 , pp. 165-184
    • Ikai, A.1    Fish, W.W.2    Tanford, C.3
  • 17
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • H. Roder, G.A. Elöve, and S.W. Englander Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR Nature 335 1988 700 704
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 18
    • 0025203243 scopus 로고
    • Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
    • M.-F. Jeng, S.W. Englander, G.A. Elöve, A.J. Wand, and H. Roder Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR Biochemistry 29 1990 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
  • 21
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • G.A. Elöve, A.K. Bhuyan, and H. Roder Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands Biochemistry 33 1994 6925 6935
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 22
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Y. Bai, T.R. Sosnick, L. Mayne, and S.W. Englander Protein folding intermediates: native-state hydrogen exchange Science 269 1995 192 197
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 23
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • T. Pascher, J.P. Chesick, J.R. Winkler, and H.B. Gray Protein folding triggered by electron transfer Science 271 1996 1558 1560
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 25
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • M.C.R. Shastry, and H. Roder Evidence for barrier-limited protein folding kinetics on the microsecond time scale Nature Struct. Biol. 5 1998 385 392
    • (1998) Nature Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 26
    • 0015154226 scopus 로고
    • The existence of heme-protein-coordinate-covalent bonds in denaturing solvents
    • J. Babul, and E. Stellwagen The existence of heme-protein-coordinate- covalent bonds in denaturing solvents Biopolymers 10 1971 2359 2361
    • (1971) Biopolymers , vol.10 , pp. 2359-2361
    • Babul, J.1    Stellwagen, E.2
  • 27
    • 0016390528 scopus 로고
    • Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c
    • J.A. Knapp, and C.N. Pace Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c Biochemistry 13 1974 1289 1294
    • (1974) Biochemistry , vol.13 , pp. 1289-1294
    • Knapp, J.A.1    Pace, C.N.2
  • 28
    • 0017824058 scopus 로고
    • Equilibrium and kinetic studies of unfolding of homologous cytochromes c
    • G. McLendon, and M. Smith Equilibrium and kinetic studies of unfolding of homologous cytochromes c J. Biol. Chem. 253 1978 4004 4008
    • (1978) J. Biol. Chem. , vol.253 , pp. 4004-4008
    • McLendon, G.1    Smith, M.2
  • 29
    • 0025967568 scopus 로고
    • Multifrequency calorimetry of the folding/unfolding transition of cytochrome c
    • W.W. van Osdol, O.L. Mayorga, and E. Freire Multifrequency calorimetry of the folding/unfolding transition of cytochrome c Biophys. J. 59 1991 48 54
    • (1991) Biophys. J. , vol.59 , pp. 48-54
    • Van Osdol, W.W.1    Mayorga, O.L.2    Freire, E.3
  • 30
    • 0034682478 scopus 로고    scopus 로고
    • NMR investigation of ferricytochrome c unfolding: Detection of an equilibrium unfolding intermediate and residual structure in the denatured state
    • B.S. Russell, R. Melenkivitz, and K.L. Bren NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state Proc. Natl Acad. Sci. USA 97 2000 8312 8317
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8312-8317
    • Russell, B.S.1    Melenkivitz, R.2    Bren, K.L.3
  • 31
    • 0036928729 scopus 로고    scopus 로고
    • Denaturant dependence of equilibrium unfolding intermediates and denatured state structure of horse ferricytochrome c
    • B.S. Russell, and K.L. Bren Denaturant dependence of equilibrium unfolding intermediates and denatured state structure of horse ferricytochrome c J. Biol. Inorg. Chem. 7 2002 909 916
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 909-916
    • Russell, B.S.1    Bren, K.L.2
  • 32
    • 0042622660 scopus 로고    scopus 로고
    • Equilibrium studies of the effect of difference in sequence homology on the mechanism of denaturation of bovine and horse cytochromes-c
    • B. Moza, S.H. Qureshi, and F. Ahmad Equilibrium studies of the effect of difference in sequence homology on the mechanism of denaturation of bovine and horse cytochromes-c Biochim. Biophys. Acta 1646 2003 49 56
    • (2003) Biochim. Biophys. Acta , vol.1646 , pp. 49-56
    • Moza, B.1    Qureshi, S.H.2    Ahmad, F.3
  • 33
    • 0032497321 scopus 로고    scopus 로고
    • Protein denaturation: A small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c
    • D.J. Segel, A.L. Fink, K.O. Hodgson, and S. Doniach Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c Biochemistry 37 1998 12443 12451
    • (1998) Biochemistry , vol.37 , pp. 12443-12451
    • Segel, D.J.1    Fink, A.L.2    Hodgson, K.O.3    Doniach, S.4
  • 34
    • 0033778161 scopus 로고    scopus 로고
    • Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange
    • L. Mayne, and S.W. Englander Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange Protein Sci. 9 2000 1873 1877
    • (2000) Protein Sci. , vol.9 , pp. 1873-1877
    • Mayne, L.1    Englander, S.W.2
  • 35
    • 0025832142 scopus 로고
    • Effective concentrations of amino acid side chains in an unfolded protein
    • K. Muthukrishnan, and B.T. Nall Effective concentrations of amino acid side chains in an unfolded protein Biochemistry 30 1991 4706 4710
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nall, B.T.2
  • 36
    • 0030614407 scopus 로고    scopus 로고
    • A lysine 73 -> Histidine variant of yeast iso-1-cytochrome c: Evidence for a native-like intermediate in the unfolding pathway and implications for m value effects
    • S. Godbole, A. Dong, K. Garbin, and B.E. Bowler A lysine 73 -> histidine variant of yeast iso-1-cytochrome c: evidence for a native-like intermediate in the unfolding pathway and implications for m value effects Biochemistry 36 1997 119 126
    • (1997) Biochemistry , vol.36 , pp. 119-126
    • Godbole, S.1    Dong, A.2    Garbin, K.3    Bowler, B.E.4
  • 37
    • 26244436812 scopus 로고    scopus 로고
    • Kinetics of loop formation and breakage in the denatured state of Iso-1-cytochrome c
    • E. Kurchan, H. Roder, and B.E. Bowler Kinetics of loop formation and breakage in the denatured state of Iso-1-cytochrome c J. Mol. Biol. 353 2005 730 743
    • (2005) J. Mol. Biol. , vol.353 , pp. 730-743
    • Kurchan, E.1    Roder, H.2    Bowler, B.E.3
  • 38
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • W. Colón, L.P. Wakem, F. Sherman, and H. Roder Identification of the predominant non-native histidine ligand in unfolded cytochrome c Biochemistry 36 1997 12535 12541
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colón, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 39
    • 0037192146 scopus 로고    scopus 로고
    • Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C
    • S.J. Hagen, R.F. Latypov, D.A. Dolgikh, and H. Roder Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C Biochemistry 41 2002 1372 1380
    • (2002) Biochemistry , vol.41 , pp. 1372-1380
    • Hagen, S.J.1    Latypov, R.F.2    Dolgikh, D.A.3    Roder, H.4
  • 41
    • 0000058698 scopus 로고
    • Charge-transfer optical spectra, electron paramagnetic resonance, and redox potentials of cytochromes
    • A. Schejter, and W.A. Eaton Charge-transfer optical spectra, electron paramagnetic resonance, and redox potentials of cytochromes Biochemistry 23 1984 1081 1084
    • (1984) Biochemistry , vol.23 , pp. 1081-1084
    • Schejter, A.1    Eaton, W.A.2
  • 43
    • 0014171978 scopus 로고
    • Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformation
    • E. Schechter, and P. Saludjian Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformation Biopolymers 5 1967 788 790
    • (1967) Biopolymers , vol.5 , pp. 788-790
    • Schechter, E.1    Saludjian, P.2
  • 44
    • 0016380496 scopus 로고
    • The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation
    • T.Y. Tsong The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation J. Biol. Chem. 249 1974 1988 1990
    • (1974) J. Biol. Chem. , vol.249 , pp. 1988-1990
    • Tsong, T.Y.1
  • 45
    • 0019319092 scopus 로고
    • Urea denaturation of horse heart ferricytochrome c. Equilibrium studies and characterization of intermediate forms
    • Y.P. Myer, L.H. MacDonald, B.C. Verma, and A. Pande Urea denaturation of horse heart ferricytochrome c. Equilibrium studies and characterization of intermediate forms Biochemistry 19 1980 199 207
    • (1980) Biochemistry , vol.19 , pp. 199-207
    • Myer, Y.P.1    MacDonald, L.H.2    Verma, B.C.3    Pande, A.4
  • 46
    • 0030583719 scopus 로고    scopus 로고
    • Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c
    • T. Ferri, A. Poscia, F. Ascoli, and R. Santucci Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c Biochim. Biophys. Acta 1298 1996 102 108
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 102-108
    • Ferri, T.1    Poscia, A.2    Ascoli, F.3    Santucci, R.4
  • 47
    • 0017027586 scopus 로고
    • Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group
    • T.Y. Tsong Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group Biochemistry 15 1976 5467 5473
    • (1976) Biochemistry , vol.15 , pp. 5467-5473
    • Tsong, T.Y.1
  • 48
    • 0034025695 scopus 로고    scopus 로고
    • Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies
    • Yg. Thomas, Ra. Goldbeck, and Ds. Kliger Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies Biopolymers 57 2000 29 36
    • (2000) Biopolymers , vol.57 , pp. 29-36
    • Thomas, Yg.1    Goldbeck, Ra.2    Kliger, Ds.3
  • 49
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • P.S. Kim, and R.L. Baldwin Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding Annu. Rev. Biochem. 51 1982 459 489
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 50
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • A.L. Fink 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
  • 51
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • M.M. Santoro, and D.W. Bolen A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range Biochemistry 31 1992 4901 4907
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 52
    • 0031038733 scopus 로고    scopus 로고
    • Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants
    • R.M. Ionescu, and M.R. Eftink Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants Biochemistry 36 1997 1129 1140
    • (1997) Biochemistry , vol.36 , pp. 1129-1140
    • Ionescu, R.M.1    Eftink, M.R.2
  • 53
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure
    • D. Hamada, and Y. Goto The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure J. Mol. Biol. 269 1997 479 487
    • (1997) J. Mol. Biol. , vol.269 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 54
    • 1842609473 scopus 로고    scopus 로고
    • Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing
    • K. Maki, H. Cheng, D.A. Dolgikh, M.C. Shastry, and H. Roder Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing J. Mol. Biol. 338 2004 383 400
    • (2004) J. Mol. Biol. , vol.338 , pp. 383-400
    • Maki, K.1    Cheng, H.2    Dolgikh, D.A.3    Shastry, M.C.4    Roder, H.5
  • 56
    • 0028220369 scopus 로고
    • A structural basis for the interaction of urea with lysozyme
    • A.C.W. Pike, and K.R. Acharya A structural basis for the interaction of urea with lysozyme Protein Sci. 3 1994 706 710
    • (1994) Protein Sci. , vol.3 , pp. 706-710
    • Pike, A.C.W.1    Acharya, K.R.2
  • 57
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • G.W. Bushnell, G.V. Louie, and G.D. Brayer High-resolution three-dimensional structure of horse heart cytochrome c J. Mol. Biol. 214 1990 585 595
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 58
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochrome c
    • J. Babul, and E. Stellwagen Participation of the protein ligands in the folding of cytochrome c Biochemistry 11 1972 1195 1200
    • (1972) Biochemistry , vol.11 , pp. 1195-1200
    • Babul, J.1    Stellwagen, E.2
  • 59
    • 0001861010 scopus 로고
    • Structure and stability of cytochrome c folding intermediates
    • G.A. Elöve, and H. Roder Structure and stability of cytochrome c folding intermediates ACS Symp. Ser. 470 1991 50 63
    • (1991) ACS Symp. Ser. , vol.470 , pp. 50-63
    • Elöve, G.A.1    Roder, H.2
  • 60
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme ligation
    • B. Hammack, S. Godbole, and B.E. Bowler Cytochrome c folding traps are not due solely to histidine-heme ligation: direct demonstration of a role for N-terminal amino group-heme ligation J. Mol. Biol. 275 1998 719 724
    • (1998) J. Mol. Biol. , vol.275 , pp. 719-724
    • Hammack, B.1    Godbole, S.2    Bowler, B.E.3
  • 61
    • 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
    • W. Colón, G.A. Elöve, L.P. Wakem, F. Sherman, and H. Roder Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding Biochemistry 35 1996 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
  • 62
    • 0015743054 scopus 로고
    • The appearance of transient species of cytochrome c upon rapid oxidation or reduction at alkaline pH
    • D.O. Lambeth, K.L. Campbell, R. Zand, and G. Palmer The appearance of transient species of cytochrome c upon rapid oxidation or reduction at alkaline pH J. Biol. Chem. 248 1973 8130 8136
    • (1973) J. Biol. Chem. , vol.248 , pp. 8130-8136
    • Lambeth, D.O.1    Campbell, K.L.2    Zand, R.3    Palmer, G.4
  • 63
    • 0034254338 scopus 로고    scopus 로고
    • Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c
    • F.I. Rosell, T.R. Harris, D.P. Hildebrand, S. Dopner, P. Hildebrandt, and A.G. Mauk Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c Biochemistry 39 2000 9047 9054
    • (2000) Biochemistry , vol.39 , pp. 9047-9054
    • Rosell, F.I.1    Harris, T.R.2    Hildebrand, D.P.3    Dopner, S.4    Hildebrandt, P.5    Mauk, A.G.6
  • 64
    • 0031952599 scopus 로고    scopus 로고
    • Folding intermediates in cytochrome c
    • S.-R. Yeh, and D.L. Rousseau Folding intermediates in cytochrome c Nature Struct. Biol. 5 1998 222 228
    • (1998) Nature Struct. Biol. , vol.5 , pp. 222-228
    • Yeh, S.-R.1    Rousseau, D.L.2
  • 65
    • 0032766705 scopus 로고    scopus 로고
    • Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c
    • J.S. Milne, Y. Xu, L.C. Mayne, and S.W. Englander Experimental study of the protein folding landscape: unfolding reactions in cytochrome c J. Mol. Biol. 290 1999 811 822
    • (1999) J. Mol. Biol. , vol.290 , pp. 811-822
    • Milne, J.S.1    Xu, Y.2    Mayne, L.C.3    Englander, S.W.4
  • 69
    • 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
    • D. Hamada, Y. Kuroda, M. Kataoka, S. Aimoto, T. Yoshimura, and Y. Goto Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c J. Mol. Biol. 256 1996 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
  • 70
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by small angle X-ray scattering
    • M. Kataoka, Y. Hagihara, K. Mihara, and Y. Goto 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
  • 71
    • 0016256727 scopus 로고
    • Alkaline isomerization of oxidized cytochrome c. Equilibrium and kinetic measurements
    • L. Davis, A. Schejter, and G.P. Hess Alkaline isomerization of oxidized cytochrome c. Equilibrium and kinetic measurements J. Biol. Chem. 249 1974 2624 2632
    • (1974) J. Biol. Chem. , vol.249 , pp. 2624-2632
    • Davis, L.1    Schejter, A.2    Hess, G.P.3
  • 72
    • 0034619421 scopus 로고    scopus 로고
    • PH dependence of formation of a partially unfolded state of a Lys 73→His variant of iso-1-cytochrome c: Implications for the alkaline conformational transition of cytochrome c
    • C.J. Nelson, and B.E. Bowler pH dependence of formation of a partially unfolded state of a Lys 73→His variant of iso-1-cytochrome c: implications for the alkaline conformational transition of cytochrome c Biochemistry 39 2000 13584 13594
    • (2000) Biochemistry , vol.39 , pp. 13584-13594
    • Nelson, C.J.1    Bowler, B.E.2
  • 73
    • 0034821575 scopus 로고    scopus 로고
    • Direct detection of heat and cold denaturation for partial unfolding of a protein
    • C.J. Nelson, M.J. LaConte, and B.E. Bowler Direct detection of heat and cold denaturation for partial unfolding of a protein J. Am. Chem. Soc. 123 2001 7453 7454
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7453-7454
    • Nelson, C.J.1    Laconte, M.J.2    Bowler, B.E.3
  • 75
  • 77
    • 0034737327 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • S.J. Hagen, and W.A. Eaton Two-state expansion and collapse of a polypeptide J. Mol. Biol. 297 2000 781 789
    • (2000) J. Mol. Biol. , vol.297 , pp. 781-789
    • Hagen, S.J.1    Eaton, W.A.2
  • 79
    • 0542421561 scopus 로고    scopus 로고
    • Kinetic and structural analysis of submillisecond folding events in cytochrome c
    • M.C.R. Shastry, J.M. Sauder, and H. Roder Kinetic and structural analysis of submillisecond folding events in cytochrome c Acc. Chem. Res. 31 1998 717 725
    • (1998) Acc. Chem. Res. , vol.31 , pp. 717-725
    • Shastry, M.C.R.1    Sauder, J.M.2    Roder, H.3
  • 85
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • W.B.R. Pollock, F.I. Rosell, M.B. Twitchett, M.E. Dumont, and A.G. Mauk Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition Biochemistry 37 1998 6124 6131
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.R.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 86
    • 0030207171 scopus 로고    scopus 로고
    • An optimized 3D NOESY-HSQC
    • S. Talluri, and G. Wagner An optimized 3D NOESY-HSQC J. Magn. Reson. 112 1996 200 205
    • (1996) J. Magn. Reson. , vol.112 , pp. 200-205
    • Talluri, S.1    Wagner, G.2
  • 87
    • 0028545648 scopus 로고
    • Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • H. Kuboniwa, S. Grzesiek, F. Delaglio, and A. Bax Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods J. Biomol. NMR 4 1994 871 878
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 90
    • 0001594959 scopus 로고
    • Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients
    • A. Bax, and S.S. Pochapsky Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients J. Magn. Reson. 99 1992 638 643
    • (1992) J. Magn. Reson. , vol.99 , pp. 638-643
    • Bax, A.1    Pochapsky, S.S.2


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