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Volumn 39, Issue 4, 2000, Pages 758-761

Rigid aniphiphiles for membrane protein manipulation

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOPHILE; BACTERIORHODOPSIN; MEMBRANE PROTEIN; RHODOPSIN;

EID: 0034681577     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1521-3773(20000218)39:4<758::aid-anie758>3.0.co;2-v     Document Type: Article
Times cited : (71)

References (64)
  • 22
    • 36849148472 scopus 로고
    • The structure of detergents have been difficult to analyze in membrane protein crystals, because of extensive disorder. Only a handful of such studies have been reported: a) M. Roth, L.-A. Bentley, H. Michel, J. Deisenhofer, R. Huber, D. Oesterhclt, Nature 1989, 340, 659;
    • (1989) Nature , vol.340 , pp. 659
    • Roth, M.1    Bentley, L.-A.2    Michel, H.3    Deisenhofer, J.4    Huber, R.5    Oesterhclt, D.6
  • 34
  • 39
    • 0000664301 scopus 로고
    • b) H. Michel, EMBO J. 1982, 1, 1267;
    • (1982) EMBO J. , vol.1 , pp. 1267
    • Michel, H.1
  • 63
    • 33745139492 scopus 로고    scopus 로고
    • note
    • The total amount of Rho present was estimated from the difference in the spectral absorbance at 500 nm before and after bleaching for 15 min under a white light.
  • 64
    • 0032478818 scopus 로고    scopus 로고
    • which were grown with LDAO
    • + channel from Streptomyces lividans can be crystallized in the presence of this tripod amphiphile. These crystals, however, do not diffract X-rays as well as the crystals used for the published 3.2 Å-resolution structure of this protein (D. A. Doyle, J. M. Cabral, R. A. Pruetzner, A. L. Kuo, J. M. Gulbis, S. L. Cohen, B. T. Chait, R. Mackinnon, Science 1998, 280, 69), which were grown with LDAO.
    • (1998) Science , vol.280 , pp. 69
    • Doyle, D.A.1    Cabral, J.M.2    Pruetzner, R.A.3    Kuo, A.L.4    Gulbis, J.M.5    Cohen, S.L.6    Chait, B.T.7    Mackinnon, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.