메뉴 건너뛰기




Volumn 7, Issue 5, 1998, Pages 1071-1082

Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force

Author keywords

Free energy; Global suppressors; Iso 2 cytochrome c; Protein folding; Yeast

Indexed keywords

ASPARAGINE; CYTOCHROME C; GUANIDINE; ISOLEUCINE; SOLVENT;

EID: 0031862845     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070501     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0028220311 scopus 로고
    • The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c
    • Berghuis AM, Guillemette JG, McLendon G, Sherman F, Smith M, Brayer GD. 1994. The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c. J Mol Biol 236:786-799.
    • (1994) J Mol Biol , vol.236 , pp. 786-799
    • Berghuis, A.M.1    Guillemette, J.G.2    McLendon, G.3    Sherman, F.4    Smith, M.5    Brayer, G.D.6
  • 2
    • 0025822952 scopus 로고
    • Genetic analysis of yeast iso-1-cytochrome c structural requirements: Suppression of Gly6 replacements by an Asn52-Ile replacement
    • Berroteran RW, Hampsey M. 1991. Genetic analysis of yeast iso-1-cytochrome c structural requirements: Suppression of Gly6 replacements by an Asn52-Ile replacement. Arch Biochem Biophys 288:261-269.
    • (1991) Arch Biochem Biophys , vol.288 , pp. 261-269
    • Berroteran, R.W.1    Hampsey, M.2
  • 3
    • 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
    • Colon W, Elove GA, Wakem LP, 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
    • Colon, W.1    Elove, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 4
    • 0343170500 scopus 로고
    • Dramatic thermostabilization of yeasl iso-1 -cytochrome c by an asparagine-isoleucine replacement at position 57
    • Das G, Hickey DR, McLendon D, McLendon G, Sherman F. 1989. Dramatic thermostabilization of yeasl iso-1 -cytochrome c by an asparagine-isoleucine replacement at position 57. Proc Natl Acad Sci USA 56:496-499.
    • (1989) Proc Natl Acad Sci USA , vol.56 , pp. 496-499
    • Das, G.1    Hickey, D.R.2    McLendon, D.3    McLendon, G.4    Sherman, F.5
  • 6
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elove GA, Bhuyan AK, 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
    • Elove, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 7
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elove GA, Chaffotte AF, Roder H, Goldberg ME. 1992. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry 37:6876-6883.
    • (1992) Biochemistry , vol.37 , pp. 6876-6883
    • Elove, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 9
    • 0027163998 scopus 로고
    • The sixth Datta lecture. Protein folding and stability: The pathway of folding of barnase
    • Fersht AR. 1993. The sixth Datta lecture. Protein folding and stability: The pathway of folding of barnase. FEBS Lett 325:5-16.
    • (1993) FEBS Lett , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 10
    • 0026526794 scopus 로고
    • Electron-proton coupling in cytochrome c studied using protein variants
    • Gao Y, McLendon G, Pielak GJ, Williams RJ. 1992. Electron-proton coupling in cytochrome c studied using protein variants. Eur J Biochem 204:337-352.
    • (1992) Eur J Biochem , vol.204 , pp. 337-352
    • Gao, Y.1    McLendon, G.2    Pielak, G.J.3    Williams, R.J.4
  • 12
    • 0015918913 scopus 로고
    • Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c
    • Ikai A, Fish WW, Tanford C. 1973. Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c. J Mol Biol 73:165-184.
    • (1973) J Mol Biol , vol.73 , pp. 165-184
    • Ikai, A.1    Fish, W.W.2    Tanford, C.3
  • 13
    • 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 ID, Roder H. 1996. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat Struct Biol 3:193-205.
    • (1996) Nat Struct Biol , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 14
    • 0016390528 scopus 로고
    • Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c
    • Knapp JA, Pace CN. 1974. Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c. Biochemistry 13:1289-1294.
    • (1974) Biochemistry , vol.13 , pp. 1289-1294
    • Knapp, J.A.1    Pace, C.N.2
  • 15
    • 0028064464 scopus 로고
    • Thermodynamics of the equilibrium unfolding of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochromes c
    • Komar-Panicucci S, Weis D, Bakker G, Qiao T, Sherman F, McLendon G. 1994. Thermodynamics of the equilibrium unfolding of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochromes c. Biochemistry 33:10556-10560.
    • (1994) Biochemistry , vol.33 , pp. 10556-10560
    • Komar-Panicucci, S.1    Weis, D.2    Bakker, G.3    Qiao, T.4    Sherman, F.5    McLendon, G.6
  • 17
    • 0025146477 scopus 로고
    • High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes r
    • Louie GV, Brayer GD. 1990. High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes r. J Mol Biol 214:527-555.
    • (1990) J Mol Biol , vol.214 , pp. 527-555
    • Louie, G.V.1    Brayer, G.D.2
  • 18
    • 0027171034 scopus 로고
    • Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding
    • Matouschek A, Fersht AR. 1993. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc Natl Acad Sci USA 90:7814-7818.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7814-7818
    • Matouschek, A.1    Fersht, A.R.2
  • 19
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek A, Kellis JJ, Serrano L, Bycroft M, Fersht AR. 1990. Transient folding intermediates characterized by protein engineering. Nature 346:440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis, J.J.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 20
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Malouschek A, Kellis JJ, Serrano L, Fersht AR. 1989. Mapping the transition state and pathway of protein folding by protein engineering. Nature 340:122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Malouschek, A.1    Kellis, J.J.2    Serrano, L.3    Fersht, A.R.4
  • 21
    • 0029041315 scopus 로고
    • Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: Observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase
    • Matthews JM, Fersht AR. 1995. Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: Observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase. Biochemistry 34:6805-6814.
    • (1995) Biochemistry , vol.34 , pp. 6805-6814
    • Matthews, J.M.1    Fersht, A.R.2
  • 24
    • 0026760321 scopus 로고
    • Structure determination and analysis of yeast iso-2-cytochrome c and a composite mutant protein
    • Murphy ME, Nall BT, Brayer GD. 1992. Structure determination and analysis of yeast iso-2-cytochrome c and a composite mutant protein. J Mol Biol 227:160-176.
    • (1992) J Mol Biol , vol.227 , pp. 160-176
    • Murphy, M.E.1    Nall, B.T.2    Brayer, G.D.3
  • 26
    • 0028820703 scopus 로고
    • Denaturant in values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM. 1995. Denaturant in 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
  • 27
    • 0020641070 scopus 로고
    • Structural intermediates in folding of yeast iso-2 cytochrome c
    • Nall BT. 1983. Structural intermediates in folding of yeast iso-2 cytochrome c. Biochemistry 22:1423-1429.
    • (1983) Biochemistry , vol.22 , pp. 1423-1429
    • Nall, B.T.1
  • 28
    • 0043143394 scopus 로고    scopus 로고
    • Cytochrome r folding and stability
    • Scott RA, Mauk AG, eds. Sausalito: University Science Books.
    • Nall BT. 1996. Cytochrome r folding and stability. In: Scott RA, Mauk AG, eds. Cytochrome c. A multidisciplinary approach. Sausalito: University Science Books. pp 167-200.
    • (1996) Cytochrome C. A Multidisciplinary Approach , pp. 167-200
    • Nall, B.T.1
  • 29
    • 0019849938 scopus 로고
    • Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c
    • Nall BT, Landers TA. 1981. Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c. Biochemistry 20:5403-5411.
    • (1981) Biochemistry , vol.20 , pp. 5403-5411
    • Nall, B.T.1    Landers, T.A.2
  • 30
    • 0024293192 scopus 로고
    • pH dependence of folding of iso-2-cytochrome c
    • Nall BT, Osterhout JJ, Ramdas L. 1988. pH dependence of folding of iso-2-cytochrome c. Biochemistry 27:7310-7314.
    • (1988) Biochemistry , vol.27 , pp. 7310-7314
    • Nall, B.T.1    Osterhout, J.J.2    Ramdas, L.3
  • 31
    • 0022323072 scopus 로고
    • Slow refolding kinetics in yeast iso-2 cytochrome c
    • Osterhout JJ, Nall BT. 1985. Slow refolding kinetics in yeast iso-2 cytochrome c. Biochemistry 24:7999-8005.
    • (1985) Biochemistry , vol.24 , pp. 7999-8005
    • Osterhout, J.J.1    Nall, B.T.2
  • 32
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 33
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reacuons
    • Parker MJ, Spencer J, Clarke AR. 1995. An integrated kinetic analysis of intermediates and transition states in protein folding reacuons. J Mol Biol 253:771-786.
    • (1995) J Mol Biol , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 34
    • 0030897736 scopus 로고    scopus 로고
    • Fast folding of cytochrome c
    • Pierce MM, Nall BT. 1997. Fast folding of cytochrome c. Protein Sci 6:618-627.
    • (1997) Protein Sci , vol.6 , pp. 618-627
    • Pierce, M.M.1    Nall, B.T.2
  • 36
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 38
    • 0021968408 scopus 로고
    • Genetic analysis of staphylococcal nuclease: Identification of three intragenic global suppressors of nuclease-minus mutants
    • Shortle D, Lin B. 1985. Genetic analysis of staphylococcal nuclease: Identification of three intragenic global suppressors of nuclease-minus mutants. Genetics 110:539-555.
    • (1985) Genetics , vol.110 , pp. 539-555
    • Shortle, D.1    Lin, B.2
  • 41
    • 0016769984 scopus 로고
    • An acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutions
    • Tsong TY. 1975. An acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutions. Biochemistry 14:1542-1547.
    • (1975) Biochemistry , vol.14 , pp. 1542-1547
    • Tsong, T.Y.1
  • 42
    • 0017027586 scopus 로고
    • Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group
    • Tsong TY. 1976. Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group. Biochemistry 15:5467-5473.
    • (1976) Biochemistry , vol.15 , pp. 5467-5473
    • Tsong, T.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.