메뉴 건너뛰기




Volumn 62, Issue 3, 2007, Pages 258-264

A stopped-flow fluorescence study of the native and modified lysozyme

Author keywords

value; Bioinformatics; Folding; Hen egg white lysozyme; Stopped flow kinetics; Transition state

Indexed keywords

VERTEBRATA;

EID: 50849125125     PISSN: 00063088     EISSN: 13369563     Source Type: Journal    
DOI: 10.2478/s11756-007-0045-0     Document Type: Article
Times cited : (2)

References (54)
  • 4
    • 0026793589 scopus 로고
    • Kinetic resolution of peptide bond and side-chain far UV CD during folding of HEWL
    • Caffotte A.F., Guillou Y & Goldberg M.E. 1992. Kinetic resolution of peptide bond and side-chain far UV CD during folding of HEWL. Biochemistry 31: 9694-9702.
    • (1992) Biochemistry , vol.31 , pp. 9694-9702
    • Caffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 5
    • 0032512697 scopus 로고    scopus 로고
    • Kinetics of lysozyme refolding: Structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering
    • Chen L., Wildegger G., Kiefhaber T.H., Hodgson K.O & Doniach S. 1998. Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering. J. Mol. Biol. 276: 225-237.
    • (1998) J. Mol. Biol. , vol.276 , pp. 225-237
    • Chen, L.1    Wildegger, G.2    Kiefhaber, T.H.3    Hodgson, K.O.4    Doniach, S.5
  • 6
    • 0032570532 scopus 로고    scopus 로고
    • Folding intermediates of wild-type and mutants of barnase: Use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium
    • Dalby P.A, Oliveberg M. & Fersht A.R. 1998. Folding intermediates of wild-type and mutants of barnase: use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium. J. Mol. Biol. 276: 625-646.
    • (1998) J. Mol. Biol. , vol.276 , pp. 625-646
    • Dalby, P.A.1    Oliveberg, M.2    Fersht, A.R.3
  • 8
    • 0027936262 scopus 로고
    • Kinetics of folding of guanidinic denatured hen egg white lysozyme and carboxymethyl Cys(6).Cys(12r)-lysozyme: A stopped-flow absorbance and fluorescence study
    • Denton M.E., Rothwarf D.M & Scheraga H.A. 1994. Kinetics of folding of guanidinic denatured hen egg white lysozyme and carboxymethyl Cys(6).Cys(12r)-lysozyme: a stopped-flow absorbance and fluorescence study. Biochemistry 33: 11225-11236.
    • (1994) Biochemistry , vol.33 , pp. 11225-11236
    • Denton, M.E.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 9
    • 0014325267 scopus 로고
    • Reversible blocking of amino groups with citraconic anhydride
    • Dixon H.B.F & Perham R.N. 1968. Reversible blocking of amino groups with citraconic anhydride. Biochem. J. 109: 312-314.
    • (1968) Biochem. J. , vol.109 , pp. 312-314
    • Dixon, H.B.F.1    Perham, R.N.2
  • 10
    • 37049147605 scopus 로고
    • Some applications of the transition state method to the calculation of reaction velocities, especially in solution
    • Evans M.G & Polanyi M. 1935. Some applications of the transition state method to the calculation of reaction velocities, especially in solution. Trans. Faraday Soc. 31: 875-894.
    • (1935) Trans. Faraday Soc. , vol.31 , pp. 875-894
    • Evans, M.G.1    Polanyi, M.2
  • 11
    • 1342296307 scopus 로고
    • The activated complex and the absolute rate of chemical reactions
    • Eyring H. 1935. The activated complex and the absolute rate of chemical reactions. Chem. Rev. 17: 65-77.
    • (1935) Chem. Rev. , vol.17 , pp. 65-77
    • Eyring, H.1
  • 12
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • Fersht A.R. 1993. 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
  • 13
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht A.R. 1997. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7: 3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 14
    • 0026511656 scopus 로고
    • The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A.R., Matouscheck A & Serrano L. 1992. The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224: 771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouscheck, A.2    Serrano, L.3
  • 15
    • 0031822735 scopus 로고    scopus 로고
    • Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond
    • Ikeguchi M., Fujino M., Kato M., Kuwajima K & Sugai S. 1998. Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond. Protein Sci. 7: 1564-1574.
    • (1998) Protein Sci. , vol.7 , pp. 1564-1574
    • Ikeguchi, M.1    Fujino, M.2    Kato, M.3    Kuwajima, K.4    Sugai, S.5
  • 16
    • 0015343130 scopus 로고
    • Fluorescence of lysozyme: Emission from tryptophan residues 62 and 108 and energy migration
    • Imoto T., Forster L.S., Rupley J.A & Tanak F. 1981. Fluorescence of lysozyme: emission from tryptophan residues 62 and 108 and energy migration. Proc. Natl. Acad. Sci. USA 69: 1151-1155.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1151-1155
    • Imoto, T.1    Forster, L.S.2    Rupley, J.A.3    Tanak, F.4
  • 17
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probs
    • Itzhaki L.S., Evans P.A., Dobson C.M. & Radford S.E. 1994. Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probs. Biochemistry 33: 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
  • 18
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • Jolles P & Jolles J. 1984. What's new in lysozyme research? Mol. Cell. Biochem. 63: 165-189.
    • (1984) Mol. Cell. Biochem. , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 19
    • 0020475131 scopus 로고
    • Identification and characterization of the direct folding process of hen egg white lysozyme
    • Kato S., Shimoto N. & Utijma H. 1982. Identification and characterization of the direct folding process of hen egg white lysozyme. Biochemistry 21: 38-43.
    • (1982) Biochemistry , vol.21 , pp. 38-43
    • Kato, S.1    Shimoto, N.2    Utijma, H.3
  • 21
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber T. 1995. Kinetic traps in lysozyme folding. Proc. Natl. Acad. Sci. USA 92: 9029-9033.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 22
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Kiefhaber T & Wildegger G. 1997. Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270: 294-304.
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Kiefhaber, T.1    Wildegger, G.2
  • 23
    • 0022423885 scopus 로고
    • Comparison of the transition state folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima K., Hiraoka Y., Ikeguchi M & Sugai S. 1985. Comparison of the transition state folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24: 874-881
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 24
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A., Kellis J., Serrano L & Fersht A.R. 1989. Mapping the transition state and pathway of protein folding by protein engineering. Nature 340: 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, J.2    Serrano, L.3    Fersht, A.R.4
  • 25
    • 0026550397 scopus 로고
    • The folding of an enzyme: IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure
    • Matouschek A., Serrano L. & Fersht A.R. 1992. The folding of an enzyme: IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224: 819-835.
    • (1992) J. Mol. Biol. , vol.224 , pp. 819-835
    • Matouschek, A.1    Serrano, L.2    Fersht, A.R.3
  • 26
    • 0026524680 scopus 로고
    • The folding of an enzyme: V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: Complementarity to and agreement with protein engineering studies
    • Matouschek A., Serrano L., Meiering E.M., Bycroft M. & Fersht A.R. 1992. The folding of an enzyme: V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies. J. Mol. Biol. 224: 837-845.
    • (1992) J. Mol. Biol. , vol.224 , pp. 837-845
    • Matouschek, A.1    Serrano, L.2    Meiering, E.M.3    Bycroft, M.4    Fersht, A.R.5
  • 28
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved positions in protein folds: Reading evolutionary signals about stability, folding and function
    • Mirny L.A & Shakhnovich E.I. 1999. Universally conserved positions in protein folds: reading evolutionary signals about stability, folding and function. J. Mol. Biol. 291: 177-196.
    • (1999) J. Mol. Biol. , vol.291 , pp. 177-196
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 30
    • 0035957514 scopus 로고    scopus 로고
    • Evolutionary conservation of the folding nucleus
    • Mirny L.A & Shakhnovich E.I. 2001b. Evolutionary conservation of the folding nucleus. J. Mol. Biol. 308: 123-129.
    • (2001) J. Mol. Biol. , vol.308 , pp. 123-129
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 31
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 33
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transitions states in protein folding reactions
    • Parker M.J., Spencer J & Clark A.R. 1995. An integrated kinetic analysis of intermediates and transitions states in protein folding reactions. J. Mol. Biol. 253: 771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clark, A.R.3
  • 35
    • 0033004893 scopus 로고    scopus 로고
    • Predicting the protein folding nucleus from a sequence
    • Poupon A. & Marnon J.P. 1999. Predicting the protein folding nucleus from a sequence. FEBS Lett. 452: 283-289.
    • (1999) FEBS Lett. , vol.452 , pp. 283-289
    • Poupon, A.1    Marnon, J.P.2
  • 37
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S.E., Dobson C.M & Evans P.A. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358: 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 38
    • 0027482860 scopus 로고
    • Structural consequences of reductive methylation of lysine residue in hen egg white lysozyme: An X-ray analysis at 1.8-? resolution
    • Rypniech W.R., Holden H.M & Rayment I. 1993. Structural consequences of reductive methylation of lysine residue in hen egg white lysozyme: an X-ray analysis at 1.8-? resolution. Biochemistry 32: 9851-9858.
    • (1993) Biochemistry , vol.32 , pp. 9851-9858
    • Rypniech, W.R.1    Holden, H.M.2    Rayment, I.3
  • 39
    • 0345826034 scopus 로고    scopus 로고
    • Solution-and crystal-phase covalent modification of lysozyme by a purpose-designed organoruthenium complex. A MALDI-TOF MS study of its metal binding sites
    • Salmine M., Caro B., Guen-Robin F.L., Blais J.C & Jaouen G. 2004. Solution-and crystal-phase covalent modification of lysozyme by a purpose-designed organoruthenium complex. A MALDI-TOF MS study of its metal binding sites. ChemBioChem 5: 99-109.
    • (2004) ChemBioChem , vol.5 , pp. 99-109
    • Salmine, M.1    Caro, B.2    Guen-Robin, F.L.3    Blais, J.C.4    Jaouen, G.5
  • 40
    • 0028263356 scopus 로고
    • Measurement of barnase refolding rate constants under denaturing conditions
    • Sanz J.M & Fersht A.R. 1994. Measurement of barnase refolding rate constants under denaturing conditions, FEBS Lett. 344: 216-220.
    • (1994) FEBS Lett. , vol.344 , pp. 216-220
    • Sanz, J.M.1    Fersht, A.R.2
  • 41
    • 0000814919 scopus 로고
    • Direct determination of absolute circular dichroism data and calibration of commercial instrument
    • Schippers P.H & Deckers H.P.J.M. 1981. Direct determination of absolute circular dichroism data and calibration of commercial instrument. Anal. Chem. 53: 778-788.
    • (1981) Anal. Chem. , vol.53 , pp. 778-788
    • Schippers, P.H.1    Deckers, H.P.J.M.2
  • 42
    • 0033532201 scopus 로고    scopus 로고
    • Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
    • Segel D.J., Bachmann A., Hofrichter J., Hodgson K.O & Daniach S. 1999. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. J. Mol. Biol. 288: 489-499.
    • (1999) J. Mol. Biol. , vol.288 , pp. 489-499
    • Segel, D.J.1    Bachmann, A.2    Hofrichter, J.3    Hodgson, K.O.4    Daniach, S.5
  • 43
    • 0026553768 scopus 로고
    • The folding of an enzyme: II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano L., Kellis J., Cann T.P., Matouschek A & Fersht A.R. 1992. The folding of an enzyme: II. Substructure of barnase and the contribution of different interactions to protein stability. J. Mol. Biol. 224: 783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.2    Cann, T.P.3    Matouschek, A.4    Fersht, A.R.5
  • 44
    • 0026579572 scopus 로고
    • The folding of an enzyme: III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
    • Serrano L., Matouschek A & Fersht A.R. 1992. The folding of an enzyme: III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224: 805-818.
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 45
    • 0026563495 scopus 로고
    • The folding of an enzyme: IV. the folding pathway of barnase: Comparison with theoretical models
    • Serrano L., Matouschek A & Fersht, A.R. 1992. The folding of an enzyme: IV. The folding pathway of barnase: comparison with theoretical models. J. Mol. Biol. 224: 847-850.
    • (1992) J. Mol. Biol. , vol.224 , pp. 847-850
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 46
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich E.I., Abkevich V.I & Ptitsyn O. 1996. Conserved residues and the mechanism of protein folding. Nature 379: 96-98.
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.I.1    Abkevich, V.I.2    Ptitsyn, O.3
  • 48
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau D., Mak M & Przybylski M. 1992. Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. USA 89: 5630-5634.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 49
    • 84998283298 scopus 로고
    • New standard substance for calibration of circular dichroism: Ammoniumd-10-camphorsulfonate
    • Takakuwa T., Konno T & Meguro H.A. 1985. New standard substance for calibration of circular dichroism: ammoniumd-10-camphorsulfonate. Anal. Sci. 1: 215-225.
    • (1985) Anal. Sci. , vol.1 , pp. 215-225
    • Takakuwa, T.1    Konno, T.2    Meguro, H.A.3
  • 50
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. 1968. Protein denaturation. Adv. Protein Chem. 23: 121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 51
    • 0014718113 scopus 로고
    • Protein denaturation
    • Tanford C. 1970. Protein denaturation. Adv. Protein Chem. 24: 1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 52
    • 0015918873 scopus 로고
    • Kinetics of unfolding and refolding of proteins. III: Results for lysozyme
    • Tanford C., Aune K.C & Ikai A.A. 1973. Kinetics of unfolding and refolding of proteins. III: Results for lysozyme. J. Mol. Biol. 73: 185-197.
    • (1973) J. Mol. Biol. , vol.73 , pp. 185-197
    • Tanford, C.1    Aune, K.C.2    Ikai, A.A.3
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G & Gibson T.J. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.