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Volumn 5, Issue 1, 1996, Pages 140-146

Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme

Author keywords

folding kinetics; isotope effect; lysozyme; protein folding

Indexed keywords

EGG WHITE; LYSOZYME;

EID: 0030061411     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050117     Document Type: Article
Times cited : (43)

References (23)
  • 5
    • 84985653913 scopus 로고
    • 1H-NMR titration shifts for studies of polypeptide conformation
    • 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers 18:299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bundi, A.1    Wüthrich, K.2
  • 6
    • 0026793589 scopus 로고
    • Kinetic resolution of peptide bond and side chain far-UV CD during the folding of hen egg-white lysozyme
    • Chaffotte AF, Guillou Y, Goldberg ME. 1992. Kinetic resolution of peptide bond and side chain far-UV CD during the folding of hen egg-white lysozyme. Biochemistry 31:9694-9703.
    • (1992) Biochemistry , vol.31 , pp. 9694-9703
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 14
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki LS, Evans PA, Dobson CM, Radford SE. 1994. Tertiary interactions in the folding of hen lysozyme: Kinetic studies using fluorescent probes. 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
  • 15
    • 0017251893 scopus 로고
    • Protein folding dynamics
    • Karplus M, Weaver DL. 1976. Protein folding dynamics. Nature 260:404-406.
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 17
    • 0023056528 scopus 로고
    • Effects of denaturants on amide proton exchange rates: A test for structure in protein fragments and folding intermediates
    • Loftus D, Gbenle GO, Kim PS, Baldwin RL. 1986. Effects of denaturants on amide proton exchange rates: A test for structure in protein fragments and folding intermediates. Biochemistry 25:1428-1436.
    • (1986) Biochemistry , vol.25 , pp. 1428-1436
    • Loftus, D.1    Gbenle, G.O.2    Kim, P.S.3    Baldwin, R.L.4
  • 19
  • 20
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford SE, Dobson CM, Evans PA. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358:102-301.
    • (1992) Nature , vol.358 , pp. 102-301
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 21
    • 0021525532 scopus 로고
    • Characterisation of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state
    • Segawa S, Sugihara M. 1984. Characterisation of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state. Biopolymers 23:2473-2488.
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.1    Sugihara, M.2
  • 22
    • 0013553240 scopus 로고
    • Thermodynamics of conformational changes of proteins. I. pH dependent denaturation of muramidase
    • Sophianopoulos AJ, Weiss BJ. 1964. Thermodynamics of conformational changes of proteins. I. pH dependent denaturation of muramidase Biochemistry 3:1920-1928.
    • (1964) Biochemistry , vol.3 , pp. 1920-1928
    • Sophianopoulos, A.J.1    Weiss, B.J.2
  • 23
    • 0000668606 scopus 로고
    • Deuterium isotope effects on protolytic dissociation of organic acids in electronically excited states
    • Wehry EL, Rogers LB. 1966. Deuterium isotope effects on protolytic dissociation of organic acids in electronically excited states. J Am Chem Soc 88:351-355.
    • (1966) J Am Chem Soc , vol.88 , pp. 351-355
    • Wehry, E.L.1    Rogers, L.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.