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Volumn 5, Issue 3, 1998, Pages 229-235

Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins

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EID: 0031890195     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0398-229     Document Type: Article
Times cited : (288)

References (55)
  • 1
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P.S. & Baldwin, R.L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489 (1982).
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 2
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S. & Baldwin, R.L. Intermediates in the folding reactions of small proteins, Annu. Rev. Biochem. 59, 631-660 (1990).
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 3
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. Folding and association of proteins. Prog. Biophys. molec. Biol. 49, 117-237 (1987).
    • (1987) Prog. Biophys. Molec. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 4
    • 0024417964 scopus 로고
    • The molten globule as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. The molten globule as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct. Funct. Genet. 6, 87-103 (1989).
    • (1989) Proteins Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 5
    • 0027313673 scopus 로고
    • Pathways of Protein Folding
    • Matthews, C.R. Pathways of Protein Folding. Annu. Rev. Biochem. 62, 653-683 (1993).
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 7
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber, T. Kinetic traps in lysozyme folding. Proc. Natl. Acad. Sci. USA 92, 9029-9033 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 8
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R.L. The nature of protein folding pathways: The classical versus the new view. J. Biomolec. NMR 5, 103-109 (1995).
    • (1995) J. Biomolec. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 9
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R.L. On-pathway versus off-pathway folding intermediates. Folding & Design 1, R1-R8 (1996).
    • (1996) Folding & Design , vol.1
    • Baldwin, R.L.1
  • 10
    • 0029904097 scopus 로고    scopus 로고
    • Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme
    • Rothwarf, D.M. & Scheraga, H.A. Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry 35, 13797-13807 (1996).
    • (1996) Biochemistry , vol.35 , pp. 13797-13807
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 11
    • 0015918856 scopus 로고
    • Kinetics of unfolding and refolding of proteins. I. Mathematical analysis
    • Ikai, A. & Tanford, C. Kinetics of unfolding and refolding of proteins. I. Mathematical analysis. J. Mol. Biol. 73, 145-163 (1973).
    • (1973) J. Mol. Biol. , vol.73 , pp. 145-163
    • Ikai, A.1    Tanford, C.2
  • 12
    • 0015918913 scopus 로고
    • Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c
    • Ikai, A., Fish, W.W. & Tanford, C. Kinetics of unfolding and refolding of proteins. II. Results for cytochrome c. J. Mol. Biol. 73, 165-184 (1973).
    • (1973) J. Mol. Biol. , vol.73 , pp. 165-184
    • Ikai, A.1    Fish, W.W.2    Tanford, C.3
  • 13
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S.E. & Fersht, A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30, 10428-10435 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 14
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
    • Jackson, S.E., elMasry, N. & Fersht, A.R. Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis. Biochemistry 32, 11270-1278 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    Elmasry, N.2    Fersht, A.R.3
  • 15
    • 0029049321 scopus 로고
    • Extremely rapid folding in the absence of intermediates: The cold-shock protein from Bacillus subtilis
    • Schindler, T., Herrler, M., Marahiel, M.A. & Schmid, F.X. Extremely rapid folding in the absence of intermediates: the cold-shock protein from Bacillus subtilis. Nature Struct. Biol. 2, 663-673 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 663-673
    • Schindler, T.1    Herrler, M.2    Marahiel, M.A.3    Schmid, F.X.4
  • 16
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler, T. & Schmid, F.X. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry 35, 16833-16842 (1996).
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 17
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric lambda represser
    • Huang, G.S. & Oas, T.G, Submillisecond folding of monomeric lambda represser. Proc. Nalt. Acad. Sci. USA 92, 6878-6882 (1995).
    • (1995) Proc. Nalt. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 19
  • 20
    • 0029965111 scopus 로고    scopus 로고
    • Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family
    • Kragelund, B.B. et al. Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family. J. Mol. Biol. 256, 187-200 (1996).
    • (1996) J. Mol. Biol. , vol.256 , pp. 187-200
    • Kragelund, B.B.1
  • 21
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
    • Viguera, A.R., Martinez, J.C., Filimonov, V.V., Mateo, P.L. & Serrano, L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry 32, 2142-2150 (1994).
    • (1994) Biochemistry , vol.32 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 22
    • 0028788480 scopus 로고
    • Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas, V. et al. Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry 34, 15105-15110 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1
  • 23
    • 0030755502 scopus 로고    scopus 로고
    • Absence of a stable intermediate on the folding pathway of protein A
    • Bai, Y.W., Karim, A., Dyson, H.J. & Wright, P.E. Absence of a stable intermediate on the folding pathway of protein A. Prot. Sci. 6, 1449-1457 (1997).
    • (1997) Prot. Sci. , vol.6 , pp. 1449-1457
    • Bai, Y.W.1    Karim, A.2    Dyson, H.J.3    Wright, P.E.4
  • 24
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones, P.G., van Bogelen, R.A. & Neidhardt, F.C. Induction of proteins in response to low temperature in Escherichia coli. J. Bacteriol. 169, 2092-2095 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 2092-2095
    • Jones, P.G.1    Van Bogelen, R.A.2    Neidhardt, F.C.3
  • 25
    • 0026648953 scopus 로고
    • Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperature
    • Willimsky, G., Bang, H., Fischer, G. & Marahiel, M.A. Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperature. J. Bacteriol. 174, 6326-6335 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 6326-6335
    • Willimsky, G.1    Bang, H.2    Fischer, G.3    Marahiel, M.A.4
  • 26
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
    • Schindelin, H., Marahiel, M.A. & Heinemann, U. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 364, 164-168 (1993).
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 27
    • 0027248819 scopus 로고
    • Structure in solution of the major cold-shock protein from Bacillus subtilis
    • Schnuchel, A. et al. Structure in solution of the major cold-shock protein from Bacillus subtilis. Nature 364, 169-171 (1993).
    • (1993) Nature , vol.364 , pp. 169-171
    • Schnuchel, A.1
  • 28
    • 0015918873 scopus 로고
    • Kinetics of unfolding and refolding of proteins. III. Results for lysozyme
    • Tanford, C., Aune, K.C. & Ikai, A. Kinetics of unfolding and refolding of proteins. III. Results for lysozyme. J. Mol. Biol.73, 185-197 (1973).
    • (1973) J. Mol. Biol. , vol.73 , pp. 185-197
    • Tanford, C.1    Aune, K.C.2    Ikai, A.3
  • 29
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A., Kellis, J.T., Serrano, L., Bycroft, M. & Fersht, A.R. Transient folding intermediates characterized by protein engineering. Nature 346, 440-445 (1990).
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 30
    • 0027163998 scopus 로고
    • Protein Folding and Stability - The Pathway of Folding of Barnase
    • Fersht, A.R. Protein Folding and Stability - The Pathway of Folding of Barnase. FEBS Lett. 325, 5-16 (1993).
    • (1993) FEBS Lett , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 31
    • 0027305989 scopus 로고
    • Folding and Stability of a Tryptophan-Containing Mutant of Ubiquitin
    • Khorasanizadeh, S., Peters, I.D., Butt T.R. & Roder, H. Folding and Stability of a Tryptophan-Containing Mutant of Ubiquitin. Biochemistry 32, 7054-7063 (1993).
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 32
    • 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. 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).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 33
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colon, W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 34
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G. & Kiefhaber, T. Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270, 294-304 (1997).
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 36
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C
    • Huber, R. et al. Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C. Arch. Microbiol. 144, 324-333 (1986).
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1
  • 39
    • 0038933138 scopus 로고    scopus 로고
    • Folding of the disulfide-bonded beta-sheet protein tendamistat; Rapid two-state folding without hydrophobic collapse
    • Scho&nbrunner, N., Koller, K.P. & Kiefhaber, T. Folding of the disulfide-bonded beta-sheet protein tendamistat; Rapid two-state folding without hydrophobic collapse J. Mol. Biol. 268, 526-538 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 526-538
    • Schonbrunner, N.1    Koller, K.P.2    Kiefhaber, T.3
  • 40
    • 0031574916 scopus 로고    scopus 로고
    • Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all-beta sheet alpha-spectrin SH3 domain
    • Prieto, J., Wilmanns, M., Jiménez, M.A., Rico, M. & Serrano, L Non-native local interactions in protein folding and stability: introducing a helical tendency in the all-beta sheet alpha-spectrin SH3 domain. J. Mol. Biol. 268, 760-778 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 760-778
    • Prieto, J.1    Wilmanns, M.2    Jiménez, M.A.3    Rico, M.4    Serrano, L.5
  • 41
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A.R., Serrano, L. & Wilmanns, M. Different folding transition states may result in the same native structure. Nature Struct. Biol. 3, 874-880 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 42
    • 0028882589 scopus 로고
    • P22 arc represser: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • Milla, M.E., Brown, B.M., Waldburgen, C.D. & Sauer, R.T. P22 arc represser: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry 34, 13914-13919 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburgen, C.D.3    Sauer, R.T.4
  • 45
    • 0031837168 scopus 로고    scopus 로고
    • Protein folding: Matching 'theory' and experiment
    • in the press
    • Laurents, D.V. & Baldwin, R.L. Protein folding: matching 'theory' and experiment. Biophys. J. in the press (1998).
    • (1998) Biophys. J.
    • Laurents, D.V.1    Baldwin, R.L.2
  • 46
    • 0030334626 scopus 로고    scopus 로고
    • Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model
    • Mirny, L.A., Abkevich, V. & Shakhnovich, E.I. Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of a lattice model. Folding & Design 1, 103-116 (1996).
    • (1996) Folding & Design , vol.1 , pp. 103-116
    • Mirny, L.A.1    Abkevich, V.2    Shakhnovich, E.I.3
  • 47
  • 48
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich, E., Abkevich, V. & Ptitsyn, O. Conserved residues and the mechanism of protein folding. Nature 379, 96-98 (1996).
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 49
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Meth. Enz. 131, 266-280 (1986).
    • (1986) Meth. Enz. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 50
    • 0026642589 scopus 로고
    • Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB
    • Schindelin, H., Herrler, M., Willimsky, G., Marahiel, M.A. & Heinemann, U. Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB, Proteins Struct. Funct. Genet 14, 120-124 (1992).
    • (1992) Proteins Struct. Funct. Genet , vol.14 , pp. 120-124
    • Schindelin, H.1    Herrler, M.2    Willimsky, G.3    Marahiel, M.A.4    Heinemann, U.5
  • 51
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. & von Hippel, P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326 (1989).
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 52
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, CM., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. How to measure and predict the molar absorption coefficient of a protein. Prot. Sci. 4, 2411-2423 (1995).
    • (1995) Prot. Sci. , vol.4 , pp. 2411-2423
    • Pace, C.M.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 53
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl αchymotrypsin using different denaturants
    • Santoro, M.M. & Bolen, D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl αchymotrypsin using different denaturants. Biochemistry 27, 8063-8068 (1988).
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 55
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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