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Volumn 376, Issue 5, 2008, Pages 1451-1462

Kinetic Folding of Haloferax volcanii and Escherichia coli Dihydrofolate Reductases: Haloadaptation by Unfolded State Destabilization at High Ionic Strength

Author keywords

fluorescence; halophilic enzymes; kinetics; protein folding

Indexed keywords

DIHYDROFOLATE REDUCTASE; POTASSIUM CHLORIDE; UREA;

EID: 39149125451     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.12.056     Document Type: Article
Times cited : (15)

References (61)
  • 1
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry 29 (1990) 7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 3
    • 1242319518 scopus 로고    scopus 로고
    • Impact of protein denaturants and stabilizers on water structure
    • Batchelor J.D., Olteanu A., Tripathy A., and Pielak G.J. Impact of protein denaturants and stabilizers on water structure. J. Am. Chem. Soc. 126 (2004) 1958-1961
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1958-1961
    • Batchelor, J.D.1    Olteanu, A.2    Tripathy, A.3    Pielak, G.J.4
  • 4
    • 33749365298 scopus 로고    scopus 로고
    • A molecular mechanism for osmolyte-induced protein stability
    • Street T.O., Bolen D.W., and Rose G.D. A molecular mechanism for osmolyte-induced protein stability. Proc. Natl Acad. Sci. USA 103 (2006) 13997-14002
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 13997-14002
    • Street, T.O.1    Bolen, D.W.2    Rose, G.D.3
  • 5
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin R.L. How Hofmeister ion interactions affect protein stability. Biophys. J. 71 (1996) 2056-2063
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 6
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: salt and solvent effects on interfacial phenomena
    • Cacace M.G., Landau E.M., and Ramsden J.J. The Hofmeister series: salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 30 (1997) 241-277
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 7
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated
    • Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. (1998) 51
    • (1998) Adv. Protein Chem. , pp. 51
    • Timasheff, S.N.1
  • 8
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: how do solvents affect these processes?
    • Timasheff S.N. The control of protein stability and association by weak interactions with water: how do solvents affect these processes?. Annu. Rev. Biophys. Biomol. Struct. 22 (1993) 67-97
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 10
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectric effects, Hofmeister effects and osmotic effects of salts
    • Record M.T.J., Zhang W., and Anderson C.F. Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectric effects, Hofmeister effects and osmotic effects of salts. Adv. Protein Chem. 51 (1998) 281-353
    • (1998) Adv. Protein Chem. , vol.51 , pp. 281-353
    • Record, M.T.J.1    Zhang, W.2    Anderson, C.F.3
  • 11
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect
    • Ramos C.H., and Baldwin R.L. Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect. Protein Sci. 11 (2002) 1771-1778
    • (2002) Protein Sci. , vol.11 , pp. 1771-1778
    • Ramos, C.H.1    Baldwin, R.L.2
  • 12
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D., Mueller U., Heinemann U., and Schmid F.X. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat. Struct. Biol. 7 (2000) 380-383
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 13
  • 14
    • 0027980588 scopus 로고
    • Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state
    • Oliveberg M., Vuilleumier S., and Fersht A.R. Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. Biochemistry 33 (1994) 8826-8832
    • (1994) Biochemistry , vol.33 , pp. 8826-8832
    • Oliveberg, M.1    Vuilleumier, S.2    Fersht, A.R.3
  • 15
    • 0033852796 scopus 로고    scopus 로고
    • Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    • Pace C.N., Alston R.W., and Shaw K.L. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci. 9 (2000) 1395-1398
    • (2000) Protein Sci. , vol.9 , pp. 1395-1398
    • Pace, C.N.1    Alston, R.W.2    Shaw, K.L.3
  • 16
    • 33645034410 scopus 로고    scopus 로고
    • Molecular mechanisms of pH-driven conformational transitions of proteins: insights from continuum electrostatics calculations of acid unfolding
    • Fitch C.A., Whitten S.T., Hilser V.J., and Garcia-Moreno E.B. Molecular mechanisms of pH-driven conformational transitions of proteins: insights from continuum electrostatics calculations of acid unfolding. Proteins: Struct. Funct. Genet. 63 (2006) 113-126
    • (2006) Proteins: Struct. Funct. Genet. , vol.63 , pp. 113-126
    • Fitch, C.A.1    Whitten, S.T.2    Hilser, V.J.3    Garcia-Moreno, E.B.4
  • 17
    • 37049007026 scopus 로고    scopus 로고
    • Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation
    • Song B., Cho J.H., and Raleigh D.P. Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Biochemistry 46 (2007) 14206-14214
    • (2007) Biochemistry , vol.46 , pp. 14206-14214
    • Song, B.1    Cho, J.H.2    Raleigh, D.P.3
  • 18
    • 0000959078 scopus 로고
    • Solute concentrations within cells of halophilic and non-halophilic bacteria
    • Christian J.H.B., and Waltho J.A. Solute concentrations within cells of halophilic and non-halophilic bacteria. Biochim. Biophys. Acta 65 (1962) 506-508
    • (1962) Biochim. Biophys. Acta , vol.65 , pp. 506-508
    • Christian, J.H.B.1    Waltho, J.A.2
  • 20
    • 0028014604 scopus 로고
    • Relevance of sequence statistics for the properties of extremophilic proteins
    • Böhm G., and Jaenicke R. Relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Pept. Protein Res. 43 (1994) 97-106
    • (1994) Int. J. Pept. Protein Res. , vol.43 , pp. 97-106
    • Böhm, G.1    Jaenicke, R.2
  • 21
    • 0028084481 scopus 로고
    • A structure-based model for the halophilic adaptation of dihydrofolate reductase from Halobacterium volcanii
    • Böhm G., and Jaenicke R. A structure-based model for the halophilic adaptation of dihydrofolate reductase from Halobacterium volcanii. Protein Eng. 17 (1994) 213-220
    • (1994) Protein Eng. , vol.17 , pp. 213-220
    • Böhm, G.1    Jaenicke, R.2
  • 22
    • 0036408309 scopus 로고    scopus 로고
    • Comparison of the effects of salt on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases
    • Wright D.B., Banks D.D., Hilsenbeck J.L., Lohman J.R., and Gloss L.M. Comparison of the effects of salt on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. J. Mol. Biol. 323 (2002) 327-344
    • (2002) J. Mol. Biol. , vol.323 , pp. 327-344
    • Wright, D.B.1    Banks, D.D.2    Hilsenbeck, J.L.3    Lohman, J.R.4    Gloss, L.M.5
  • 23
    • 33645529310 scopus 로고    scopus 로고
    • Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei
    • Britton K.L., Baker P.J., Fisher M., Ruzheinikov S., Gilmour D.J., Bonete M.J., et al. Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei. Proc. Natl Acad. Sci. USA 103 (2006) 4846-4851
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4846-4851
    • Britton, K.L.1    Baker, P.J.2    Fisher, M.3    Ruzheinikov, S.4    Gilmour, D.J.5    Bonete, M.J.6
  • 24
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteria
    • Lanyi J.K. Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol. Rev. 38 (1974) 272-290
    • (1974) Bacteriol. Rev. , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 25
    • 0032563113 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of halophilic proteins
    • Elcock A.H., and McCammon J.A. Electrostatic contributions to the stability of halophilic proteins. J. Mol. Biol. 280 (1998) 731-748
    • (1998) J. Mol. Biol. , vol.280 , pp. 731-748
    • Elcock, A.H.1    McCammon, J.A.2
  • 26
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: proteins with a grain of salt
    • Mevarech M., Frolow F., and Gloss L.M. Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 86 (2000) 155-164
    • (2000) Biophys. Chem. , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 27
    • 0037459095 scopus 로고    scopus 로고
    • The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies
    • Irimia A., Ebel C., Madern D., Richard S.B., Cosenza L.W., Zaccai G., and Vellieux F.M. The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. J. Mol. Biol. 326 (2003) 859-873
    • (2003) J. Mol. Biol. , vol.326 , pp. 859-873
    • Irimia, A.1    Ebel, C.2    Madern, D.3    Richard, S.B.4    Cosenza, L.W.5    Zaccai, G.6    Vellieux, F.M.7
  • 28
    • 0032518248 scopus 로고    scopus 로고
    • Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii
    • Pieper U., Kapadia G., Mevarech M., and Herzberg O. Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii. Structure 6 (1998) 75-88
    • (1998) Structure , vol.6 , pp. 75-88
    • Pieper, U.1    Kapadia, G.2    Mevarech, M.3    Herzberg, O.4
  • 30
    • 37049069515 scopus 로고
    • A biophysical study of halophilic malate dehydrogenase in solution: revised subunit structure and solvent interactions in native and recombinant enzyme
    • Bonneté F., Ebel C., Eisenberg H., and Zaccai G. A biophysical study of halophilic malate dehydrogenase in solution: revised subunit structure and solvent interactions in native and recombinant enzyme. J. Chem. Soc., Faraday Trans. 89 (1993) 2659-2666
    • (1993) J. Chem. Soc., Faraday Trans. , vol.89 , pp. 2659-2666
    • Bonneté, F.1    Ebel, C.2    Eisenberg, H.3    Zaccai, G.4
  • 31
    • 0033551441 scopus 로고    scopus 로고
    • Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase
    • Ebel C., Faou P., Kernel B., and Zaccai G. Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase. Biochemistry 38 (1999) 9039-9047
    • (1999) Biochemistry , vol.38 , pp. 9039-9047
    • Ebel, C.1    Faou, P.2    Kernel, B.3    Zaccai, G.4
  • 32
    • 0037027318 scopus 로고    scopus 로고
    • Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptation
    • Costenaro L., Zaccai G., and Ebel C. Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptation. Biochemistry 41 (2002) 13245-13252
    • (2002) Biochemistry , vol.41 , pp. 13245-13252
    • Costenaro, L.1    Zaccai, G.2    Ebel, C.3
  • 34
    • 0034021158 scopus 로고    scopus 로고
    • The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases
    • Ortenberg R., Rozenblatt-Rosen O., and Mevarech M. The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases. Mol. Microbiol. 35 (2000) 1493-1505
    • (2000) Mol. Microbiol. , vol.35 , pp. 1493-1505
    • Ortenberg, R.1    Rozenblatt-Rosen, O.2    Mevarech, M.3
  • 35
    • 0024971668 scopus 로고
    • Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii
    • Zusman T., Rosenshine I., Boehm G., Jaenicke R., Leskiw B., and Mevarech M. Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. J. Biol. Chem. 264 (1989) 18878-18883
    • (1989) J. Biol. Chem. , vol.264 , pp. 18878-18883
    • Zusman, T.1    Rosenshine, I.2    Boehm, G.3    Jaenicke, R.4    Leskiw, B.5    Mevarech, M.6
  • 36
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence
    • Sawaya M.R., and Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36 (1997) 586-603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 38
    • 34547557942 scopus 로고    scopus 로고
    • Structure in an extreme environment: NMR at high salt
    • Binbuga B., Boroujerdi A.F., and Young J.K. Structure in an extreme environment: NMR at high salt. Protein Sci. 16 (2007) 1783-1787
    • (2007) Protein Sci. , vol.16 , pp. 1783-1787
    • Binbuga, B.1    Boroujerdi, A.F.2    Young, J.K.3
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0027315969 scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model
    • Jennings P.A., Finn B.E., Jones B.E., and Matthews C.R. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry 32 (1993) 3783-3789
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 41
    • 0034622508 scopus 로고    scopus 로고
    • Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles
    • Ionescu R.M., Smith V.F., O'Neill J.C., and Matthews C.R. Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry 39 (2000) 9540-9550
    • (2000) Biochemistry , vol.39 , pp. 9540-9550
    • Ionescu, R.M.1    Smith, V.F.2    O'Neill, J.C.3    Matthews, C.R.4
  • 42
    • 0036289101 scopus 로고    scopus 로고
    • Highly divergent dihydrofolate reductases conserve complex folding mechanisms
    • Wallace L.A., and Matthews C.R. Highly divergent dihydrofolate reductases conserve complex folding mechanisms. J. Mol. Biol. 315 (2002) 193-211
    • (2002) J. Mol. Biol. , vol.315 , pp. 193-211
    • Wallace, L.A.1    Matthews, C.R.2
  • 43
    • 33644901015 scopus 로고    scopus 로고
    • The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E. coli
    • Svensson A.K., Zitzewitz J.A., Matthews C.R., and Smith V.F. The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E. coli. Protein Eng. Des. Sel. 19 (2006) 175-185
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 175-185
    • Svensson, A.K.1    Zitzewitz, J.A.2    Matthews, C.R.3    Smith, V.F.4
  • 44
    • 0025373255 scopus 로고
    • Refolding of E. coli DHFR: sequential formation of substrate binding sites
    • Frieden C. Refolding of E. coli DHFR: sequential formation of substrate binding sites. Proc. Natl Acad. Sci. USA 87 (1990) 4413-4416
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4413-4416
    • Frieden, C.1
  • 45
    • 0033613814 scopus 로고    scopus 로고
    • Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures
    • Clark A.C., and Frieden C. Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures. J. Mol. Biol. 285 (1999) 1765-1776
    • (1999) J. Mol. Biol. , vol.285 , pp. 1765-1776
    • Clark, A.C.1    Frieden, C.2
  • 46
    • 0024784280 scopus 로고
    • A hydrophobic cluster forms early in the folding of dihydrofolate reductase
    • Garvey E.P., Swank J., and Matthews C.R. A hydrophobic cluster forms early in the folding of dihydrofolate reductase. Proteins: Struct. Funct. Genet. 6 (1989) 259-266
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 259-266
    • Garvey, E.P.1    Swank, J.2    Matthews, C.R.3
  • 47
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima K., Garvey E.P., Finn B.E., Matthews C.R., and Sugai S. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 30 (1991) 7693-7703
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 48
    • 0028947956 scopus 로고
    • Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
    • Jones B.E., and Matthews C.R. Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci. 4 (1995) 167-177
    • (1995) Protein Sci. , vol.4 , pp. 167-177
    • Jones, B.E.1    Matthews, C.R.2
  • 49
    • 0029115374 scopus 로고
    • Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates
    • Engelhard M., and Evans P.A. Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Protein Sci. 4 (1995) 1553-1562
    • (1995) Protein Sci. , vol.4 , pp. 1553-1562
    • Engelhard, M.1    Evans, P.A.2
  • 50
    • 0032534842 scopus 로고    scopus 로고
    • The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding
    • Ogasahara K., Nakamura M., Nakura S., Tsunasawa S., Kato I., Yoshimoto T., and Yutani K. The unusually slow unfolding rate causes the high stability of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus: equilibrium and kinetic studies of guanidine hydrochloride-induced unfolding and refolding. Biochemistry 37 (1998) 17537-17544
    • (1998) Biochemistry , vol.37 , pp. 17537-17544
    • Ogasahara, K.1    Nakamura, M.2    Nakura, S.3    Tsunasawa, S.4    Kato, I.5    Yoshimoto, T.6    Yutani, K.7
  • 51
    • 0036290245 scopus 로고    scopus 로고
    • The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus
    • Kaushik J.K., Ogasahara K., and Yutani K. The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus. J. Mol. Biol. 316 (2002) 991-1003
    • (2002) J. Mol. Biol. , vol.316 , pp. 991-1003
    • Kaushik, J.K.1    Ogasahara, K.2    Yutani, K.3
  • 52
    • 0032502317 scopus 로고    scopus 로고
    • Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins
    • Cavagnero S., Debe D.A., Zhou Z.H., Adams M.W., and Chan S.I. Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins. Biochemistry 37 (1998) 3369-3376
    • (1998) Biochemistry , vol.37 , pp. 3369-3376
    • Cavagnero, S.1    Debe, D.A.2    Zhou, Z.H.3    Adams, M.W.4    Chan, S.I.5
  • 53
    • 0026719686 scopus 로고
    • Global analysis of biochemical and biophysical data
    • Beechem J.M. Global analysis of biochemical and biophysical data. Methods Enzymol. 210 (1992) 37-54
    • (1992) Methods Enzymol. , vol.210 , pp. 37-54
    • Beechem, J.M.1
  • 54
    • 0035812633 scopus 로고    scopus 로고
    • Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels
    • Gloss L., Simler B., and Matthews C. Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. J. Mol. Biol. 312 (2001) 1121-1134
    • (2001) J. Mol. Biol. , vol.312 , pp. 1121-1134
    • Gloss, L.1    Simler, B.2    Matthews, C.3
  • 55
    • 0033580679 scopus 로고    scopus 로고
    • Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots
    • Otzen D.E., Kristensen O., Proctor M., and Oliveberg M. Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots. Biochemistry 38 (1999) 6499-6511
    • (1999) Biochemistry , vol.38 , pp. 6499-6511
    • Otzen, D.E.1    Kristensen, O.2    Proctor, M.3    Oliveberg, M.4
  • 56
    • 34249933886 scopus 로고    scopus 로고
    • Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability
    • Kelch B.A., and Agard D.A. Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability. J. Mol. Biol. 370 (2007) 784-795
    • (2007) J. Mol. Biol. , vol.370 , pp. 784-795
    • Kelch, B.A.1    Agard, D.A.2
  • 58
    • 13844299144 scopus 로고    scopus 로고
    • The family feud: do proteins with similar structures fold via the same pathway?
    • Zarrine-Afsar A., Larson S.M., and Davidson A.R. The family feud: do proteins with similar structures fold via the same pathway?. Curr. Opin. Struct. Biol. 15 (2005) 42-49
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 42-49
    • Zarrine-Afsar, A.1    Larson, S.M.2    Davidson, A.R.3
  • 59
    • 0028952263 scopus 로고
    • A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli
    • Iwakura M., Jones B.E., Luo J., and Matthews C.R. A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J. Biochem. 117 (1995) 480-488
    • (1995) J. Biochem. , vol.117 , pp. 480-488
    • Iwakura, M.1    Jones, B.E.2    Luo, J.3    Matthews, C.R.4
  • 60
    • 0027272686 scopus 로고
    • High expression in Escherichia coli of the gene coding for dihydrofolate reductase of the extremely halophilic archaebacterium Haloferax volcanii
    • Blecher O., Goldman S., and Mevarech M. High expression in Escherichia coli of the gene coding for dihydrofolate reductase of the extremely halophilic archaebacterium Haloferax volcanii. Eur. J. Biochem. 216 (1993) 199-203
    • (1993) Eur. J. Biochem. , vol.216 , pp. 199-203
    • Blecher, O.1    Goldman, S.2    Mevarech, M.3
  • 61
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy
    • Zitzewitz J.A., Bilsel O., Luo J., Jones B.E., and Matthews C.R. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry 34 (1995) 12812-12819
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsel, O.2    Luo, J.3    Jones, B.E.4    Matthews, C.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.