메뉴 건너뛰기




Volumn 9, Issue 1, 2000, Pages 194-196

Kinetic evidence of an on-pathway intermediate in the folding of lysozyme

Author keywords

Hen egg white lysozyme; Off pathway intermediate; On pathway intermediate; Protein folding pathway

Indexed keywords

LYSOZYME;

EID: 0033958642     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.194     Document Type: Article
Times cited : (22)

References (16)
  • 1
    • 13044284157 scopus 로고    scopus 로고
    • Kinetic evidence for an on-pathway intermediate of cytochrome c
    • Bai Y. 1999. Kinetic evidence for an on-pathway intermediate of cytochrome c. Proc Natl Acad Sci USA 96:477-480.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 477-480
    • Bai, Y.1
  • 2
    • 0028067152 scopus 로고
    • Protein stability parameters measured by hydrogen exchange
    • Bai Y, Milne JS, Mayne L, Englander SW. 1994. Protein stability parameters measured by hydrogen exchange. Proteins 20:4-14.
    • (1994) Proteins , vol.20 , pp. 4-14
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 3
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin RL. 1995. The nature of protein folding pathways: The classical versus the new view. J Biol NMR 5:103-109.
    • (1995) J Biol NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 4
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin RL. 1996. On-pathway versus off-pathway folding intermediates. Fold Design 1:1-8.
    • (1996) Fold Design , vol.1 , pp. 1-8
    • Baldwin, R.L.1
  • 5
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspectives: Chevron plots and non-Arrhenius kinetics
    • Chan HS, Dill KA. 1998. Protein folding in the landscape perspectives: Chevron plots and non-Arrhenius kinetics. Proteins 30:2-33.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 6
    • 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
  • 7
    • 0031837168 scopus 로고    scopus 로고
    • Protein folding: Matching theory and experiment
    • Laurents DV, Baldwin RL. 1998. Protein folding: Matching theory and experiment. Biophys J 75:428-434.
    • (1998) Biophys J , vol.75 , pp. 428-434
    • Laurents, D.V.1    Baldwin, R.L.2
  • 8
    • 0032582479 scopus 로고    scopus 로고
    • A pulse-chase-competition experiment to determine if a folding intermediate is on or off-pathway: Application to ribonuclease A
    • Laurents DV, Bruix MJ, Jamin M, Baldwin RL. 1998. A pulse-chase-competition experiment to determine if a folding intermediate is on or off-pathway: Application to ribonuclease A. J Mol Biol 283:669-678.
    • (1998) J Mol Biol , vol.283 , pp. 669-678
    • Laurents, D.V.1    Bruix, M.J.2    Jamin, M.3    Baldwin, R.L.4
  • 9
    • 0026729426 scopus 로고
    • Protein interaction with urea and guanidinium chloride: A calorimetric study
    • Makhatadze GI, Privalov PL. 1992. Protein interaction with urea and guanidinium chloride: A calorimetric study. J Mol Biol 226:491-505.
    • (1992) J Mol Biol , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 10
    • 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 SE, Dobson CM. 1997. Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process. J Mol Biol 227:1068-1074.
    • (1997) J Mol Biol , vol.227 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 11
    • 0028168139 scopus 로고
    • Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solution
    • Matouschek A, Matthews JM, Johnson CM, Fersht AR. 1994. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solution. Protein Eng 7:1089-1095.
    • (1994) Protein Eng , vol.7 , pp. 1089-1095
    • Matouschek, A.1    Matthews, J.M.2    Johnson, C.M.3    Fersht, A.R.4
  • 12
    • 0032499639 scopus 로고    scopus 로고
    • Characterization of collapsed states in the early stages of the refolding of hen lysozyme
    • Morgan CJ, Miranker A, Dobson CM. 1998. Characterization of collapsed states in the early stages of the refolding of hen lysozyme. Biochemistry 37:8473-8480.
    • (1998) Biochemistry , vol.37 , pp. 8473-8480
    • Morgan, C.J.1    Miranker, A.2    Dobson, C.M.3
  • 13
    • 0014939368 scopus 로고
    • The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
    • Nozaki Y, Tanford C. 1970. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions. J Biol Chem 245:1648-1652.
    • (1970) J Biol Chem , vol.245 , pp. 1648-1652
    • Nozaki, Y.1    Tanford, C.2
  • 14
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 15
    • 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 358:302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 16
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger G, Kiefhaber T. 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
    • Wildegger, G.1    Kiefhaber, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.