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Volumn 36, Issue 6, 2007, Pages 581-588

Refolding of a membrane protein in a microfluidics reactor

Author keywords

Bacteriorhodopsin; Green fluorescent protein; Membrane protein refolding; Microfluidics reactor; Structural genomics

Indexed keywords

BACTERIORHODOPSIN; DODECYL SULFATE SODIUM; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; UREA;

EID: 34347372073     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-006-0125-z     Document Type: Article
Times cited : (7)

References (41)
  • 2
    • 33645509371 scopus 로고    scopus 로고
    • Magnetic resonance investigations of lipid motion in isotropic bicelles
    • Andersson A, Maler L (2005) Magnetic resonance investigations of lipid motion in isotropic bicelles. Langmuir 21:7702-7709
    • (2005) Langmuir , vol.21 , pp. 7702-7709
    • Andersson, A.1    Maler, L.2
  • 3
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase
    • Armstrong N, de Lencastre A, Gouaux E (1999) A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase. Protein Sci 8:1475-1483
    • (1999) Protein Sci , vol.8 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 4
    • 0037648337 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1
    • Baneres JL, Martin A, Hullot P, Girard JP, Rossi JC, Parello J (2003) Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J Mol Biol 329:801-814
    • (2003) J Mol Biol , vol.329 , pp. 801-814
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 5
    • 0037450573 scopus 로고    scopus 로고
    • The trials and tribulations of membrane protein folding in vitro
    • Booth PJ (2003) The trials and tribulations of membrane protein folding in vitro. Biochim Biophys Acta 1610:51-56
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 51-56
    • Booth, P.J.1
  • 6
    • 0029943869 scopus 로고    scopus 로고
    • Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin
    • Booth PJ, Farooq A, Flitsch SL (1996) Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin. Biochemistry 35:5902-5909
    • (1996) Biochemistry , vol.35 , pp. 5902-5909
    • Booth, P.J.1    Farooq, A.2    Flitsch, S.L.3
  • 8
    • 0027465627 scopus 로고
    • Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein
    • Cody CW, Prasher DC, Westler WM, Prendergast FG, Ward WW (1993) Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 32:1212-1218
    • (1993) Biochemistry , vol.32 , pp. 1212-1218
    • Cody, C.W.1    Prasher, D.C.2    Westler, W.M.3    Prendergast, F.G.4    Ward, W.W.5
  • 9
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • Dayel MJ, Hom EF, Verkman AS (1999) Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys J 76:2843-2851
    • (1999) Biophys J , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Hom, E.F.2    Verkman, A.S.3
  • 10
    • 84977586068 scopus 로고
    • Uber die von der molekularkinetischen Theorie der Wärme gefordete Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen
    • Einstein A (1905) Uber die von der molekularkinetischen Theorie der Wärme gefordete Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen. Ann Phys 17:549-560
    • (1905) Ann Phys , vol.17 , pp. 549-560
    • Einstein, A.1
  • 11
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A, Muller DJ (2000) Observing single biomolecules at work with the atomic force microscope. Nat Struct Biol 7:715-718
    • (2000) Nat Struct Biol , vol.7 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 12
    • 8344290520 scopus 로고    scopus 로고
    • Acid denaturation and refolding of green fluorescent protein
    • Enoki S, Saeki K, Maki K, Kuwajima K (2004) Acid denaturation and refolding of green fluorescent protein. Biochemistry 43:14238-14248
    • (2004) Biochemistry , vol.43 , pp. 14238-14248
    • Enoki, S.1    Saeki, K.2    Maki, K.3    Kuwajima, K.4
  • 13
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda H, Arai M, Kuwajima K (2000) Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 39:12025-12032
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 15
    • 0030126226 scopus 로고    scopus 로고
    • Semiconductor lithography for the next millennium
    • Geppert L (1996) Semiconductor lithography for the next millennium. IEEE Spectr 33:33-38
    • (1996) IEEE Spectr , vol.33 , pp. 33-38
    • Geppert, L.1
  • 17
    • 0001391616 scopus 로고
    • A study of the diffusion of urea in water at 25-degrees with the Gouy interference method
    • Gosting LJ, Akeley DF (1952) A study of the diffusion of urea in water at 25-degrees with the Gouy interference method. J Am Chem Soc 74:2058-2060
    • (1952) J Am Chem Soc , vol.74 , pp. 2058-2060
    • Gosting, L.J.1    Akeley, D.F.2
  • 18
    • 0027218962 scopus 로고
    • Hydrophobic amino-acids in the retinal-binding pocket of bacteriorhodopsin
    • Greenhalgh DA, Farrens DL, Subramaniam S, Khorana HG (1993) Hydrophobic amino-acids in the retinal-binding pocket of bacteriorhodopsin. J Biol Chem 268:20305-20311
    • (1993) J Biol Chem , vol.268 , pp. 20305-20311
    • Greenhalgh, D.A.1    Farrens, D.L.2    Subramaniam, S.3    Khorana, H.G.4
  • 19
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • Haupts U, Tittor J, Oesterhelt D (1999) Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu Rev Biophys Biomol Struct 28:367-399
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 22
    • 17144470204 scopus 로고
    • Extending optical lithography to the gigabit era
    • Levenson MD (1995) Extending optical lithography to the gigabit era. Solid State Technol 38:57-66
    • (1995) Solid State Technol , vol.38 , pp. 57-66
    • Levenson, M.D.1
  • 23
    • 0016156057 scopus 로고
    • Intermolecular energy transfer in the bioluminescent system of Aequorea
    • Morise H, Shimomura O, Johnson FH, Winant J (1974) Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13:2656-2662
    • (1974) Biochemistry , vol.13 , pp. 2656-2662
    • Morise, H.1    Shimomura, O.2    Johnson, F.H.3    Winant, J.4
  • 25
    • 3242708681 scopus 로고    scopus 로고
    • The molecular mechanism of membrane proteins probed by evanescent infrared waves
    • Nyquist RM, Ataka K, Heberle J (2004) The molecular mechanism of membrane proteins probed by evanescent infrared waves. Chembiochem 5:431-436
    • (2004) Chembiochem , vol.5 , pp. 431-436
    • Nyquist, R.M.1    Ataka, K.2    Heberle, J.3
  • 26
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D, Stoeckenius W (1974) Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol 31:667-678
    • (1974) Methods Enzymol , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 27
    • 0000024936 scopus 로고
    • Resolution limits of optical lithography
    • Okazaki S (1991) Resolution limits of optical lithography. J Vac Sci Technol B 9:2829-2833
    • (1991) J Vac Sci Technol B , vol.9 , pp. 2829-2833
    • Okazaki, S.1
  • 28
    • 0032055340 scopus 로고    scopus 로고
    • Measurement of SDS micelle-peptide association using H-1 NMR chemical shift analysis and pulsed field gradient NMR spectroscopy
    • Orfi L, Lin MF, Larive CK (1998) Measurement of SDS micelle-peptide association using H-1 NMR chemical shift analysis and pulsed field gradient NMR spectroscopy. Anal Chem 70:1339-1345
    • (1998) Anal Chem , vol.70 , pp. 1339-1345
    • Orfi, L.1    Lin, M.F.2    Larive, C.K.3
  • 30
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid BG, Flynn GC (1997) Chromophore formation in green fluorescent protein. Biochemistry 36:6786-6791
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 31
    • 1642493929 scopus 로고    scopus 로고
    • An automated in vitro protein folding screen applied to a human dynactin subunit
    • Scheich C, Niesen FH, Seckler R, Bussow K (2004) An automated in vitro protein folding screen applied to a human dynactin subunit. Protein Sci 13:370-380
    • (2004) Protein Sci , vol.13 , pp. 370-380
    • Scheich, C.1    Niesen, F.H.2    Seckler, R.3    Bussow, K.4
  • 32
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon AM, Curnow P, Booth PJ (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochim Biophys Acta 1666:105-117
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 33
    • 0031969090 scopus 로고    scopus 로고
    • A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale
    • Shastry MC, Luck SD, Roder H (1998) A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophys J 74:2714-2721
    • (1998) Biophys J , vol.74 , pp. 2714-2721
    • Shastry, M.C.1    Luck, S.D.2    Roder, H.3
  • 34
    • 0034665455 scopus 로고    scopus 로고
    • Design of high-throughput methods of protein production for structural biology
    • Stevens RC (2000) Design of high-throughput methods of protein production for structural biology. Structure 8:R177-R185
    • (2000) Structure , vol.8
    • Stevens, R.C.1
  • 36
    • 33644841156 scopus 로고    scopus 로고
    • Fluid mixing in planar spiral microchannels
    • Sudarsan AP, Ugaz VM (2006) Fluid mixing in planar spiral microchannels. Lab Chip 6:74-82
    • (2006) Lab Chip , vol.6 , pp. 74-82
    • Sudarsan, A.P.1    Ugaz, V.M.2
  • 37
    • 0030010795 scopus 로고    scopus 로고
    • Dual roles of DMPC and CHAPS in the refolding of bacterial opsins in vitro
    • Sugiyama Y, Mukohata Y (1996) Dual roles of DMPC and CHAPS in the refolding of bacterial opsins in vitro. J Biochem 119:1143-1149
    • (1996) J Biochem , vol.119 , pp. 1143-1149
    • Sugiyama, Y.1    Mukohata, Y.2
  • 39
  • 40
    • 22144499552 scopus 로고    scopus 로고
    • Solid-state NMR in drug design and discovery for membrane-embedded targets
    • Watts A (2005) Solid-state NMR in drug design and discovery for membrane-embedded targets. Nat Rev Drug Discov 4:555-568
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 555-568
    • Watts, A.1
  • 41
    • 4043094757 scopus 로고    scopus 로고
    • A new synthetic method for controlled polymerization using a microfluidic system
    • Wu T, Mei Y, Cabral JT, Xu C, Beers KL (2004) A new synthetic method for controlled polymerization using a microfluidic system. J Am Chem Soc 126:9880-9881
    • (2004) J Am Chem Soc , vol.126 , pp. 9880-9881
    • Wu, T.1    Mei, Y.2    Cabral, J.T.3    Xu, C.4    Beers, K.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.