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Volumn 310, Issue 1, 2003, Pages 215-221

Analysis of the stability of cytochrome c6 with an improved stopped-flow protocol

Author keywords

Cytochrome c6; Kinetic analysis; Protein folding; Protein stability; Stopped flow; Urea induced denaturation

Indexed keywords

CYTOCHROME C; CYTOCHROME C6; UNCLASSIFIED DRUG;

EID: 0141849074     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.010     Document Type: Article
Times cited : (4)

References (32)
  • 1
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett V., Fersht A.R. Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28:2003;18-25.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 2
    • 0037398844 scopus 로고    scopus 로고
    • Minimalist models for protein folding and design
    • Head-Gordon T., Brown S. Minimalist models for protein folding and design. Curr. Opin. Struct. Biol. 13:2003;160-167.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 160-167
    • Head-Gordon, T.1    Brown, S.2
  • 6
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 282:2000;252-260.
    • (2000) Anal. Biochem. , vol.282 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 8
    • 0037143694 scopus 로고    scopus 로고
    • The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation
    • Shimada J., Shakhnovich E.I. The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation. Proc. Natl. Acad. Sci. USA. 99:2002;11175-11180.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11175-11180
    • Shimada, J.1    Shakhnovich, E.I.2
  • 9
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder H., Elöve G.A., Englander W. Structural characterization of folding intermediates in cytochrome. c by H-exchange labeling and proton NMR Nature. 335:1988;700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, W.3
  • 10
    • 0034685611 scopus 로고    scopus 로고
    • Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization
    • Pierce M.M., Nall B.T. Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization. J. Mol. Biol. 298:2000;955-969.
    • (2000) J. Mol. Biol. , vol.298 , pp. 955-969
    • Pierce, M.M.1    Nall, B.T.2
  • 11
    • 0037192146 scopus 로고    scopus 로고
    • Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferricytochrome c
    • Hagen S.J., Latypov R.F., Dolgikh D.A., Roder H. Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferricytochrome. 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
  • 12
    • 0028905560 scopus 로고
    • Evidence for a molten globule-like transition state in protein folding from determination of activation volumes
    • Vidugiris G.J., Markley J.L., Royer C.A. Evidence for a molten globule-like transition state in protein folding from determination of activation volumes. Biochemistry. 34:1995;4909-4912.
    • (1995) Biochemistry , vol.34 , pp. 4909-4912
    • Vidugiris, G.J.1    Markley, J.L.2    Royer, C.A.3
  • 13
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin R., Williams S., Callender R.H., Woodruff W.H., Dyer B.R. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA. 94:1997;3709-3713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, B.R.5
  • 14
    • 0034743349 scopus 로고    scopus 로고
    • ′ folding triggered by electron transfer: Fast and slow formation of four-helix bundles
    • ′ folding triggered by electron transfer: fast and slow formation of four-helix bundles Proc. Natl. Acad. Sci. USA. 98:2001;7760-7764.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7760-7764
    • Lee, J.C.1    Gray, H.B.2    Winkler, J.R.3
  • 16
    • 0037058908 scopus 로고    scopus 로고
    • Temperature jump kinetic study of the stability of apo-calmodulin
    • Rabl C.-R., Martin S.R., Neumann E., Bayley P.M. Temperature jump kinetic study of the stability of apo-calmodulin. Biophys. Chem. 101-102:2002;553-564.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 553-564
    • Rabl, C.-R.1    Martin, S.R.2    Neumann, E.3    Bayley, P.M.4
  • 17
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24:1970;1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 18
    • 0029738416 scopus 로고    scopus 로고
    • Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease a
    • Houry W.A., Rothwarf D.M., Scheraga H.A. Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease a. Biochemistry. 35:1996;10125-10133.
    • (1996) Biochemistry , vol.35 , pp. 10125-10133
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 19
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry M.C., Roder H. Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nat. Struct. Biol. 5:1998;385-392.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.1    Roder, H.2
  • 20
    • 0037160126 scopus 로고    scopus 로고
    • Kinetic intermediate in the folding of human prion protein
    • Apetri A.C., Surewicz W.K. Kinetic intermediate in the folding of human prion protein. J. Biol. Chem. 277:2002;44589-44592.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44589-44592
    • Apetri, A.C.1    Surewicz, W.K.2
  • 22
    • 0036440985 scopus 로고    scopus 로고
    • Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
    • Krantz B.A., Mayne L., Rumbley J., Englander S.W., Sosnick T.R. Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. J. Mol. Biol. 324:2002;359-371.
    • (2002) J. Mol. Biol. , vol.324 , pp. 359-371
    • Krantz, B.A.1    Mayne, L.2    Rumbley, J.3    Englander, S.W.4    Sosnick, T.R.5
  • 23
    • 0037086395 scopus 로고    scopus 로고
    • ′ -cytidine monophosphate binding affinity and enthalpy by a global fit of thermal unfolding curves
    • ′ -cytidine monophosphate binding affinity and enthalpy by a global fit of thermal unfolding curves Anal. Biochem. 302:2002;184-190.
    • (2002) Anal. Biochem. , vol.302 , pp. 184-190
    • Jones, C.L.1    Fish, F.2    Muccio, D.D.3
  • 24
    • 0031038733 scopus 로고    scopus 로고
    • Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants
    • Ionescu R.M., Eftink M.R. 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
  • 25
    • 0028168139 scopus 로고
    • Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
    • Matouschek A., Matthews J.M., Johnson C.M., Fersht A.R. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. Protein Eng. 7:1994;1089-1095.
    • (1994) Protein Eng. , vol.7 , pp. 1089-1095
    • Matouschek, A.1    Matthews, J.M.2    Johnson, C.M.3    Fersht, A.R.4
  • 26
    • 0037058957 scopus 로고    scopus 로고
    • Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curve
    • Zweifel M.E., Barrick D. Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curve. Biophys. Chem. 101-102:2002;221-237.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 221-237
    • Zweifel, M.E.1    Barrick, D.2
  • 27
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • Hammond G.S. A correlation of reaction rates. J. Am. Chem. Soc. 77:1955;334-338.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 334-338
    • Hammond, G.S.1
  • 28
    • 0035895436 scopus 로고    scopus 로고
    • Apparent two-state tendamistat folding is a sequential process along a defined route
    • Bachmann A., Kiefhaber T. Apparent two-state tendamistat folding is a sequential process along a defined route. J. Mol. Biol. 306:2001;375-386.
    • (2001) J. Mol. Biol. , vol.306 , pp. 375-386
    • Bachmann, A.1    Kiefhaber, T.2
  • 29
    • 0002203625 scopus 로고    scopus 로고
    • Kinetic models in protein folding
    • R.H. Pain. Oxford, UK: Oxford University Press
    • Bieri O., Kiefhaber T. Kinetic models in protein folding. Pain R.H. Mechanisms of Protein Folding. second ed. 2000;34-58 Oxford University Press, Oxford, UK.
    • (2000) Mechanisms of Protein Folding second ed. , pp. 34-58
    • Bieri, O.1    Kiefhaber, T.2
  • 30
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow M., Oliveberg M. High-energy channeling in protein folding. Biochemistry. 36:1997;7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 31
    • 0032503027 scopus 로고    scopus 로고
    • The changing nature of the protein folding transition state: Implications for the shape of the free-energy profile for folding
    • Oliveberg M., Tan Y.-J., Silow M., Fersht A.R. The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding. J. Mol. Biol. 277:1998;933-943.
    • (1998) J. Mol. Biol. , vol.277 , pp. 933-943
    • Oliveberg, M.1    Tan, Y.-J.2    Silow, M.3    Fersht, A.R.4
  • 32
    • 0034602677 scopus 로고    scopus 로고
    • Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements
    • Pappenberger G., Saudane C., Becker M., Merbach A.E., Kiefhaber T. Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements. Proc. Natl. Acad. Sci. USA. 97:2000;17-22.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 17-22
    • Pappenberger, G.1    Saudane, C.2    Becker, M.3    Merbach, A.E.4    Kiefhaber, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.