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Volumn 36, Issue 3, 1999, Pages 247-253

Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy

Author keywords

Chaperonin; Cytochrome c; Dissociation constant; Electrostatic interaction; Fluorescence correlation spectroscopy; GroEL; Heat shock protein; Homogeneous solution; Pepsin; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; CHAPERONIN; CYTOCHROME C; HEAT SHOCK PROTEIN; PEPSIN A;

EID: 0033168398     PISSN: 01964763     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0320(19990701)36:3<247::aid-cyto15>3.0.co;2-%23     Document Type: Article
Times cited : (48)

References (26)
  • 1
    • 0016379116 scopus 로고
    • Fluorescence correlation spectroscopy I. Conceptual basis and theory
    • Elson EL, Magde D. Fluorescence correlation spectroscopy I. Conceptual basis and theory. Biopolymers 1974;13:1-17.
    • (1974) Biopolymers , vol.13 , pp. 1-17
    • Elson, E.L.1    Magde, D.2
  • 2
    • 36749107042 scopus 로고
    • Fluorescence correlation spectroscopy as a probe of molecular dynamics
    • Aragón SR, Pecora R. Fluorescence correlation spectroscopy as a probe of molecular dynamics. J Chem Phys 1976;64:1791-1803.
    • (1976) J Chem Phys , vol.64 , pp. 1791-1803
    • Aragón, S.R.1    Pecora, R.2
  • 3
    • 0001579306 scopus 로고
    • Fluorescence correlation spectroscopy
    • Lakowicz J. editor New York: Plenum Press
    • Thompson NL. Fluorescence correlation spectroscopy. In: Lakowicz J. editor Topics in fluorescence spectroscopy. Volume 1, Techniques. New York: Plenum Press; 1991;337-374.
    • (1991) Topics in Fluorescence Spectroscopy. Volume 1, Techniques , vol.1 , pp. 337-374
    • Thompson, N.L.1
  • 4
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
    • Rigler R, Mets Ü, Widengren J, Kask P. Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur Biophys J 1993;22:169-175.
    • (1993) Eur Biophys J , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, Ü.2    Widengren, J.3    Kask, P.4
  • 5
    • 0028229903 scopus 로고
    • Sorting single molecules: Application to diagnostics and evolutionary biotechnology
    • Eigen M, Rigler R. Sorting single molecules: application to diagnostics and evolutionary biotechnology. Proc Natl Acad Sci USA 1994;91:5740-5747.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 6
    • 0029021710 scopus 로고
    • Ultrasensitive hybridization analysis using fluorescence correlation spectroscopy
    • 2.3
    • Kinjo M, Rigler R. Ultrasensitive hybridization analysis using fluorescence correlation spectroscopy. Nucleic Acids Res 1995;2.3:1795-1799.
    • (1995) Nucleic Acids Res , pp. 1795-1799
    • Kinjo, M.1    Rigler, R.2
  • 8
    • 0032126375 scopus 로고    scopus 로고
    • Single-molecule analysis of restriction DNA fragments using fluorescence correlation spectroscopy
    • Kinjo M, Nishimura G, Koyama T, Mets Ü, Rigler R. Single-molecule analysis of restriction DNA fragments using fluorescence correlation spectroscopy. Anal Biochem 1998;260:166-172.
    • (1998) Anal Biochem , vol.260 , pp. 166-172
    • Kinjo, M.1    Nishimura, G.2    Koyama, T.3    Mets, Ü.4    Rigler, R.5
  • 9
    • 0023395681 scopus 로고
    • Molecular aggregation characterized by high order autocorrelation in fluorescence correlation spectroscopy
    • Palmer AG, Thompson NL. Molecular aggregation characterized by high order autocorrelation in fluorescence correlation spectroscopy. Biophys J 1987;52:257-270.
    • (1987) Biophys J , vol.52 , pp. 257-270
    • Palmer, A.G.1    Thompson, N.L.2
  • 10
    • 0020794259 scopus 로고
    • Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy
    • Thompson NL, Axelrod D. Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy. Biophys J 1983;43:103-114.
    • (1983) Biophys J , vol.43 , pp. 103-114
    • Thompson, N.L.1    Axelrod, D.2
  • 11
    • 0030024020 scopus 로고    scopus 로고
    • Fluorescence correlation spectrometry of interaction kinetics of tetramethylrhodamine α-bungarotoxin with Torpedo California acetylcholine receptor
    • Rauer B, Neumann E, Widengren J, Rigler R. Fluorescence correlation spectrometry of interaction kinetics of tetramethylrhodamine α-bungarotoxin with Torpedo California acetylcholine receptor. Biophys Chem 1996;58:3-12.
    • (1996) Biophys Chem , vol.58 , pp. 3-12
    • Rauer, B.1    Neumann, E.2    Widengren, J.3    Rigler, R.4
  • 12
    • 0030866750 scopus 로고    scopus 로고
    • Site-specific interaction of thrombin and inhibitors observed by fluorescence correlation spectroscopy
    • Klingler J, Friedrich T. Site-specific interaction of thrombin and inhibitors observed by fluorescence correlation spectroscopy. Biophys J 1997;73:2195-2200.
    • (1997) Biophys J , vol.73 , pp. 2195-2200
    • Klingler, J.1    Friedrich, T.2
  • 13
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Elite RJ, Haiti F-U. Protein folding in the cell: competing models of chaperonin function. FASEB J 1996; 10:20-26.
    • (1996) FASEB J , vol.10 , pp. 20-26
    • Elite, R.J.1    Haiti, F.-U.2
  • 14
    • 0028792612 scopus 로고
    • Nature and consequences of GroEL-protein interactions
    • Itzhaki LS, Otzen DE, Fersht AR. Nature and consequences of GroEL-protein interactions. Biochemistry 1995;34:14581-14587.
    • (1995) Biochemistry , vol.34 , pp. 14581-14587
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 15
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL
    • Katsumata K, Okazaki A, Tsurupa GP, Kuwajima K. Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL. J Mol Biol 1996;264:643-649.
    • (1996) J Mol Biol , vol.264 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, G.P.3    Kuwajima, K.4
  • 16
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • Kuwajima K. The molten globule state of α-lactalbumin. FASEB J 1996;10:102-109.
    • (1996) FASEB J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 17
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates α-lactalbumin
    • Hayer-Hartl MK, Ewbank JJ, Creighton TE, Hartl F-U. Conformational specificity of the chaperonin GroEL for the compact folding intermediates α-lactalbumin. EMBO J 1994;13:3192-3202.
    • (1994) EMBO J , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Hartl, F.-U.4
  • 18
    • 0027318025 scopus 로고
    • Conformational instability of the N-and C-terminal lobes of porcine pepsin in neutral and alkaline solution
    • Lin X, Loy JA, Sussman F, Tang J. Conformational instability of the N-and C-terminal lobes of porcine pepsin in neutral and alkaline solution. Protein Sci 1993;2:1383-1390.
    • (1993) Protein Sci , vol.2 , pp. 1383-1390
    • Lin, X.1    Loy, J.A.2    Sussman, F.3    Tang, J.4
  • 19
    • 0030569019 scopus 로고    scopus 로고
    • Interaction of GroEL with Conformational states of horse cytochrome c
    • Hoshino M, Kawata Y, Goto Y. Interaction of GroEL with Conformational states of horse cytochrome c. J Mol Biol 1996;262:575-587.
    • (1996) J Mol Biol , vol.262 , pp. 575-587
    • Hoshino, M.1    Kawata, Y.2    Goto, Y.3
  • 20
    • 0015919686 scopus 로고
    • On the role of heme in the formation of the structure of cytochrome c
    • Fisher WR, Taniuchi H, Anfinsen CB. On the role of heme in the formation of the structure of cytochrome c. J Biol Chem 1973;248: 3188-3195.
    • (1973) J Biol Chem , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 22
    • 0031436142 scopus 로고    scopus 로고
    • Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction
    • Aoki K, Taguchi H, Shindo Y, Yoshida M, Ogasahara K, Yutani K, Tanaka N. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J Biol Chem 1997;272:32158-32162.
    • (1997) J Biol Chem , vol.272 , pp. 32158-32162
    • Aoki, K.1    Taguchi, H.2    Shindo, Y.3    Yoshida, M.4    Ogasahara, K.5    Yutani, K.6    Tanaka, N.7
  • 23
    • 0029926871 scopus 로고    scopus 로고
    • Effect of GroEL on the re-folding kinetics of a-lactalbumin
    • Katsumata K, Okazaki A, Kuwajima K. Effect of GroEL on the re-folding kinetics of a-lactalbumin. J Mol Biol 1996;258:827-838.
    • (1996) J Mol Biol , vol.258 , pp. 827-838
    • Katsumata, K.1    Okazaki, A.2    Kuwajima, K.3
  • 24
    • 0028466392 scopus 로고
    • The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
    • Okazaki A, Ikura T, Nikaido K, Kuwajima K. The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nat Struct Biol 1994;1:439-446.
    • (1994) Nat Struct Biol , vol.1 , pp. 439-446
    • Okazaki, A.1    Ikura, T.2    Nikaido, K.3    Kuwajima, K.4
  • 25
    • 0029090130 scopus 로고
    • Kinetic analysis of interactions between GroEL and reduced α-lactalbumin
    • Murai N, Taguchi H, Yoshida M. Kinetic analysis of interactions between GroEL and reduced α-lactalbumin. J Biol Chem 1995;270: 19957-19963.
    • (1995) J Biol Chem , vol.270 , pp. 19957-19963
    • Murai, N.1    Taguchi, H.2    Yoshida, M.3
  • 26
    • 0032488820 scopus 로고    scopus 로고
    • Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions
    • Brazil BT, Ybarra J, Horowitz PM. Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. J Biol Chem 1998;273:3257-3263.
    • (1998) J Biol Chem , vol.273 , pp. 3257-3263
    • Brazil, B.T.1    Ybarra, J.2    Horowitz, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.