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Volumn 277, Issue 5, 1998, Pages 997-1005

The origin of the α-domain intermediate in the folding of hen lysozyme

Author keywords

Circular dichroism; Fluorescence; Folding intermediates; Hen egg white lysozyme; Mass spectrometry; Protein folding

Indexed keywords

LYSOZYME; SODIUM CHLORIDE;

EID: 0032540326     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1657     Document Type: Article
Times cited : (48)

References (46)
  • 2
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical view versus the new view
    • Baldwin R.L. The nature of protein folding pathways the classical view versus the new view. J. Biomol. NMR. 5:1995;103-109
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 3
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin R.L. On-pathway versus off-pathway folding intermediates. Folding Des. 1:1996;R1-R8
    • (1996) Folding Des. , vol.1
    • Baldwin, R.L.1
  • 4
    • 0013852463 scopus 로고
    • Crystal structure of lysozyme by X-ray diffraction
    • Blake C.C.F., Koenig D.F., Mair G.A., Sarma R. Crystal structure of lysozyme by X-ray diffraction. Nature. 206:1965;757-761
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    Sarma, R.4
  • 5
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts J.F., Halvorson H.R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry. 14:1975;4953-4963
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 6
    • 0026793589 scopus 로고
    • Kinetic resolution of peptide bond and side chain far UV circular dichroism during the folding of hen egg white lysozyme
    • Chaffotte A.F., Guillou Y., Goldberg M.E. Kinetic resolution of peptide bond and side chain far UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry. 31:1992;9694-9702
    • (1992) Biochemistry , vol.31 , pp. 9694-9702
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 7
    • 0028402735 scopus 로고
    • The energetic ups and downs of protein folding
    • Creighton T.E. The energetic ups and downs of protein folding. Nature Stuct. Biol. 1:1994;135-138
    • (1994) Nature Stuct. Biol. , vol.1 , pp. 135-138
    • Creighton, T.E.1
  • 9
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill A.K., Chan H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, A.K.1    Chan, H.S.2
  • 10
    • 0001931668 scopus 로고
    • Unfolded proteins, compact states and molten globules
    • Dobson C.M. Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2:1992;6-12
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 6-12
    • Dobson, C.M.1
  • 11
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • Dobson C.M., Evans P.A., Radford S.E. Understanding how proteins fold the lysozyme story so far. Trends Biochem. Sci. 19:1994;31-37
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 12
    • 0344301982 scopus 로고    scopus 로고
    • Protein Folding: A Perspective from Theory & Experiment
    • In the press
    • Dobson C.M., Sali A., Karplus M. Protein Folding A Perspective from Theory & Experiment. Angew. Chem. 1998;. In the press
    • (1998) Angew. Chem.
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 13
    • 0028082357 scopus 로고
    • Probing the structure of folding intermediates
    • Evans P.A., Radford S.E. Probing the structure of folding intermediates. Curr. Opin. Struct. Biol. 4:1994;100-106
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 100-106
    • Evans, P.A.1    Radford, S.E.2
  • 14
    • 0028028126 scopus 로고
    • Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme
    • Eyles S.J., Radford S.E., Robinson C.V., Dobson C.M. Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme. Biochemistry. 33:1994;13038-13048
    • (1994) Biochemistry , vol.33 , pp. 13038-13048
    • Eyles, S.J.1    Radford, S.E.2    Robinson, C.V.3    Dobson, C.M.4
  • 15
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht A.R. Optimization of rates of protein folding the nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA. 92:1995;10869-10873
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 16
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink A.L. 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
  • 17
    • 0030322627 scopus 로고    scopus 로고
    • Structure of very early protein folding intermediates: New insights through a variant of hydrogen exchange labelling
    • Gladwin S.T., Evans P.A. Structure of very early protein folding intermediates new insights through a variant of hydrogen exchange labelling. Folding Des. 1:1996;407-417
    • (1996) Folding Des. , vol.1 , pp. 407-417
    • Gladwin, S.T.1    Evans, P.A.2
  • 18
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
    • Guo Z., Thirumalai D. Kinetics of protein folding nucleation mechanism, time scales, and pathways. Biopolymers. 36:1995;83-102
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 19
    • 0030061411 scopus 로고    scopus 로고
    • Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme
    • Itzhaki L.S., Evans P.A. Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme. Protein Sci. 5:1996;140-146
    • (1996) Protein Sci. , vol.5 , pp. 140-146
    • Itzhaki, L.S.1    Evans, P.A.2
  • 20
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki L.S., Evans P.A., Dobson C.M., Radford S.E. Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry. 33:1994;5212-5220
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 21
    • 0020475131 scopus 로고
    • Identification and characterization of the direct folding process of hen egg white lysozyme
    • Kato S., Shimamoto N., Utiyama H. Identification and characterization of the direct folding process of hen egg white lysozyme. Biochemistry. 21:1982;38-43
    • (1982) Biochemistry , vol.21 , pp. 38-43
    • Kato, S.1    Shimamoto, N.2    Utiyama, H.3
  • 22
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber T. Kinetic traps in lysozyme folding. Proc. Natl Acad. Sci. USA. 92:1995;9029-9033
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 23
    • 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. 59:1990;631-660
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 24
    • 0028936119 scopus 로고
    • Comparison of the refolding of hen lysozyme from dimethyl sulfoxide and guanidinium chloride
    • Kotik M., Radford S.E., Dobson C.M. Comparison of the refolding of hen lysozyme from dimethyl sulfoxide and guanidinium chloride. Biochemistry. 34:1995;1714-1724
    • (1995) Biochemistry , vol.34 , pp. 1714-1724
    • Kotik, M.1    Radford, S.E.2    Dobson, C.M.3
  • 25
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6:1989;87-103
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 26
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima K., Hiraoka Y., Ikeguchi M., Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:1985;874-881
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 27
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh S.N., Kay M.S., Baldwin R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl Acad. Sci. USA. 92:1995;5446-5450
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 28
    • 0031897766 scopus 로고    scopus 로고
    • The folding process of hen lysozyme: A perspective from the "new View"
    • In the press
    • Matagne A., Dobson C.M. The folding process of hen lysozyme a perspective from the "New View" Cell. Mol. Life Sci. 1998;. In the press
    • (1998) Cell. Mol. Life Sci.
    • Matagne, A.1    Dobson, C.M.2
  • 29
    • 0031576990 scopus 로고    scopus 로고
    • Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process
    • Matagne A., Radford S.E., Dobson C.M. Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process. J. Mol. Biol. 267:1997;1068-1074
    • (1997) J. Mol. Biol. , vol.267 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 30
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews C.R. Pathways of protein folding. Annu. Rev. Biochem. 62:1993;653-683
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 31
  • 32
    • 0030334626 scopus 로고    scopus 로고
    • Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a latticemodel
    • Mirny L.A., Abkevich V., Shakhnovich E.I. Universality and diversity of the protein folding scenarios a comprehensive analysis with the aid of a latticemodel. Folding Des. 1:1996;103-116
    • (1996) Folding Des. , vol.1 , pp. 103-116
    • Mirny, L.A.1    Abkevich, V.2    Shakhnovich, E.I.3
  • 33
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • Parker M.J., Spencer J., Clarke A.R. An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253:1995;771-786
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 34
    • 0030272670 scopus 로고    scopus 로고
    • Time-resolved biophysical methods in the study of protein folding
    • Plaxco K.W., Dobson C.M. Time-resolved biophysical methods in the study of protein folding. Curr. Opin. Struct. Biol. 6:1996;630-636
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 630-636
    • Plaxco, K.W.1    Dobson, C.M.2
  • 35
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47:1995;83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 36
    • 0029653893 scopus 로고
    • Insights into protein folding using physical techniques: Studies of lysozyme and α-lactalbumin
    • Radford S.E., Dobson C.M. Insights into protein folding using physical techniques studies of lysozyme and α-lactalbumin. Phil. Trans. Roy. Soc. ser. B. 348:1995;17-25
    • (1995) Phil. Trans. Roy. Soc. Ser. B , vol.348 , pp. 17-25
    • Radford, S.E.1    Dobson, C.M.2
  • 37
    • 0026751786 scopus 로고
    • The folding pathway of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S.E., Dobson C.M., Evans P.A. The folding pathway of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 38
    • 0029100019 scopus 로고
    • Watching protein folding unfold
    • Roder H. Watching protein folding unfold. Nature Stuct. Biol. 2:1995;817-820
    • (1995) Nature Stuct. Biol. , vol.2 , pp. 817-820
    • Roder, H.1
  • 39
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H., Colón W. 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
  • 40
    • 0002775727 scopus 로고
    • Early stages of protein folding
    • R.H. Pain. Oxford: Oxford University Press
    • Roder H., Elöve G.A. Early stages of protein folding. Pain R.H. Mechanisms of Protein Folding. 1994;26-54 Oxford University Press, Oxford
    • (1994) Mechanisms of Protein Folding , pp. 26-54
    • Roder, H.1    Elöve, G.A.2
  • 41
    • 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. 35:1996;13797-13807
    • (1996) Biochemistry , vol.35 , pp. 13797-13807
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 42
    • 0001340839 scopus 로고
    • Kinetics of unfolding and refolding of single-domain proteins
    • T.E. Creighton. New York: W. H. Freeman & Co
    • Schmid F.X. Kinetics of unfolding and refolding of single-domain proteins. Creighton T.E. Protein Folding. 1992;197-241 W. H. Freeman & Co, New York
    • (1992) Protein Folding , pp. 197-241
    • Schmid, F.X.1
  • 43
    • 0030768045 scopus 로고    scopus 로고
    • A residue specific view of the non-cooperative folding of a molten globule
    • 640-634
    • Schulman B., Kim P.S., Dobson C.M., Redfield C. A residue specific view of the non-cooperative folding of a molten globule. Nature Struct. Biol. 4:1997;. 640-634
    • (1997) Nature Struct. Biol. , vol.4
    • Schulman, B.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 45
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with energetically trapped intermediate
    • Wildegger G., Kiefhaber T. Three-state model for lysozyme folding: triangular folding mechanism with energetically trapped intermediate. J. Mol. Biol. 270:1997;294-304
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 46
    • 0030155292 scopus 로고    scopus 로고
    • Fast-folding experiments and the topography of protein folding energy landscapes
    • Wolynes P.G., Luthey-Schulten Z., Onuchic J.N. Fast-folding experiments and the topography of protein folding energy landscapes. Chem. Biol. 3:1996;425-432
    • (1996) Chem. Biol. , vol.3 , pp. 425-432
    • Wolynes, P.G.1    Luthey-Schulten, Z.2    Onuchic, J.N.3


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