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Volumn 119, Issue 1, 2006, Pages 78-83

Preliminary atomic force microscopy study of two-dimensional crystals of lactose permease from Escherichia coli

Author keywords

Atomic force microscopy; Lactose permease; Proteolipid sheets; Two dimensional crystallization

Indexed keywords

LACTOSE;

EID: 29344432626     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2005.07.007     Document Type: Article
Times cited : (13)

References (26)
  • 2
    • 0033977101 scopus 로고    scopus 로고
    • Families of transmembrane sugar transport proteins
    • M.H. Saier Jr. Families of transmembrane sugar transport proteins Mol. Microbiol. 35 2000 699 710
    • (2000) Mol. Microbiol. , vol.35 , pp. 699-710
    • Saier Jr., M.H.1
  • 4
    • 0032544066 scopus 로고    scopus 로고
    • The substrate-binding site in the lactose permease of Escherichia coli
    • P. Venkatesan, and H.R. Kaback The substrate-binding site in the lactose permease of Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 95 1998 9802 9807
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9802-9807
    • Venkatesan, P.1    Kaback, H.R.2
  • 6
    • 0032819684 scopus 로고    scopus 로고
    • What to do while awaiting crystals of a membrane transport protein and thereafter
    • H.R. Kaback, and J. Wu What to do while awaiting crystals of a membrane transport protein and thereafter Acc. Chem. 32 1999 805 813
    • (1999) Acc. Chem. , vol.32 , pp. 805-813
    • Kaback, H.R.1    Wu, J.2
  • 8
    • 0023666946 scopus 로고
    • Size and shape of the Escherichia coli lactose permease measured in filamentous arrays
    • J. Li, and P. Tooth Size and shape of the Escherichia coli lactose permease measured in filamentous arrays Biochemistry 26 1987 4816 4823
    • (1987) Biochemistry , vol.26 , pp. 4816-4823
    • Li, J.1    Tooth, P.2
  • 11
    • 12844271258 scopus 로고    scopus 로고
    • Atomic force microscopy study of Escherichia coli lactose permease proteolipid sheets
    • S. Merino, Ò. Domènech, M.T. Montero, and J. Hernández-Borrell Atomic force microscopy study of Escherichia coli lactose permease proteolipid sheets Biosens. Bioelectron. 20 2005 1843 1846
    • (2005) Biosens. Bioelectron. , vol.20 , pp. 1843-1846
    • Merino, S.1    Domènech, Ò.2    Montero, M.T.3    Hernández-Borrell, J.4
  • 12
    • 18844390255 scopus 로고    scopus 로고
    • Effects of lactose permease on the phospholipid environment in which it is reconstituted: A fluorescence and atomic force microscopy study
    • S. Merino, Ò. Domènech, M.T. Montero, and J. Hernández-Borrell Effects of lactose permease on the phospholipid environment in which it is reconstituted: a fluorescence and atomic force microscopy study Langmuir 21 2005 4642 4647
    • (2005) Langmuir , vol.21 , pp. 4642-4647
    • Merino, S.1    Domènech, Ò.2    Montero, M.T.3    Hernández-Borrell, J.4
  • 13
    • 23444456452 scopus 로고    scopus 로고
    • Surface thermodynamic properties of monolayers versus reconstitution of a membrane protein in solid-supported bilayers
    • (in press).
    • S. Merino, Ò. Domènech, M.T. Montero, J. Hernández-Borrell, Surface thermodynamic properties of monolayers versus reconstitution of a membrane protein in solid-supported bilayers. Colloids Surf., B Biointerfaces (in press).
    • Colloids Surf., B Biointerfaces
    • Merino, S.1    Domènech, Ò.2    Montero, M.T.3    Hernández-Borrell, J.4
  • 14
    • 0030681217 scopus 로고    scopus 로고
    • Site-directed spin-labeling of transmembrane domain VII and the 4B1 antibody epitope in the lactose permease of Escherichia coli
    • J. Voss, W.L. Hubbell, J. Hernandez-Borrell, and H.R. Kaback Site-directed spin-labeling of transmembrane domain VII and the 4B1 antibody epitope in the lactose permease of Escherichia coli Biochemistry 36 1997 15055 15061
    • (1997) Biochemistry , vol.36 , pp. 15055-15061
    • Voss, J.1    Hubbell, W.L.2    Hernandez-Borrell, J.3    Kaback, H.R.4
  • 15
    • 0033619698 scopus 로고    scopus 로고
    • Nitroxide scanning electron paramagnetic resonance of helices IV and V and the intervening loop in the lactose permease of Escherichia coli
    • M. Zhao, K.C. Zen, J. Hernandez-Borrell, C. Altenbach, W.L. Hubbell, and H.R. Kaback Nitroxide scanning electron paramagnetic resonance of helices IV and V and the intervening loop in the lactose permease of Escherichia coli Biochemistry 38 1999 15970 15977
    • (1999) Biochemistry , vol.38 , pp. 15970-15977
    • Zhao, M.1    Zen, K.C.2    Hernandez-Borrell, J.3    Altenbach, C.4    Hubbell, W.L.5    Kaback, H.R.6
  • 16
    • 0022531311 scopus 로고
    • Supported planar membranes in studies of cell-cell recognition in the immune system
    • H.M. McConnell, T.H. Watts, R.M. Weis, and A.A. Brian Supported planar membranes in studies of cell-cell recognition in the immune system Biochim. Biophys. Acta 846 1986 95 106
    • (1986) Biochim. Biophys. Acta , vol.846 , pp. 95-106
    • McConnell, H.M.1    Watts, T.H.2    Weis, R.M.3    Brian, A.A.4
  • 18
    • 0032480817 scopus 로고    scopus 로고
    • Fourier transform infrared analysis of purified lactose permease: A monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange
    • J.S. Patzlaff, J.A. Moeller, B.A. Barry, and R.J. Broker Fourier transform infrared analysis of purified lactose permease: a monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange Biochemistry 37 1998 15363 15375
    • (1998) Biochemistry , vol.37 , pp. 15363-15375
    • Patzlaff, J.S.1    Moeller, J.A.2    Barry, B.A.3    Broker, R.J.4
  • 19
    • 0037136040 scopus 로고    scopus 로고
    • Stability of the lactose permease in detergent solution
    • C.K. Engel, L. Chen, and G.G. Privé Stability of the lactose permease in detergent solution Biochim. Biophys. Acta 1564 2002 47 56
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 47-56
    • Engel, C.K.1    Chen, L.2    Privé, G.G.3
  • 20
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • D.J. Müller, M. Amreim, and A. Engel Adsorption of biological molecules to a solid support for scanning probe microscopy J. Struct. Biol. 119 1997 172 188
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.J.1    Amreim, M.2    Engel, A.3
  • 23
    • 42749103898 scopus 로고    scopus 로고
    • Atomic force microscopy contact, tapping, and jumping modes for imaging biological samples in liquids
    • F. Moreno-Herrero, J. Colchero, J. Gómez-Herrero, and A.M. Baró Atomic force microscopy contact, tapping, and jumping modes for imaging biological samples in liquids Phys. Rev., E 69 2004 031915
    • (2004) Phys. Rev., e , vol.69 , pp. 031915
    • Moreno-Herrero, F.1    Colchero, J.2    Gómez-Herrero, J.3    Baró, A.M.4
  • 24
    • 0036845373 scopus 로고    scopus 로고
    • Topology of polytopic membrane protein subdomains is dictated by membrane phospholipids composition
    • X. Wang, M. Bogdanov, and W. Dowhan Topology of polytopic membrane protein subdomains is dictated by membrane phospholipids composition EMBO J. 21 2002 5673 5681
    • (2002) EMBO J. , vol.21 , pp. 5673-5681
    • Wang, X.1    Bogdanov, M.2    Dowhan, W.3
  • 25
    • 0036470051 scopus 로고    scopus 로고
    • Protein Explorer: Easy yet powerful macromolecular visualization
    • E. Martz Protein Explorer: easy yet powerful macromolecular visualization TIBS 27 2002 107 109
    • (2002) TIBS , vol.27 , pp. 107-109
    • Martz, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.