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Volumn 119, Issue 10, 1997, Pages 2479-2487

A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines

Author keywords

[No Author keywords available]

Indexed keywords

STREPTAVIDIN;

EID: 0030901962     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja964099e     Document Type: Article
Times cited : (67)

References (43)
  • 7
    • 0342663053 scopus 로고    scopus 로고
    • Mann, S., Ed.; VCH Publishers, Inc.: New York
    • Douglas, K. In Biomimetic Materials Chemistry; Mann, S., Ed.; VCH Publishers, Inc.: New York, 1996; pp 117-142.
    • (1996) Biomimetic Materials Chemistry , pp. 117-142
    • Douglas, K.1
  • 8
    • 0015243059 scopus 로고
    • Fromherz, P. Nature 1971, 231, 267-268.
    • (1971) Nature , vol.231 , pp. 267-268
    • Fromherz, P.1
  • 31
    • 0024463575 scopus 로고
    • Polarization fluorescence microscopy of the streptavidin domains requires the protein to be labeled at a unique site. The succinimidyl ester chemistry preferentially labels lysine residues and is therefore expected to label a number of residues on the protein surface. However, the polarized fluorescence results indicate the streptavidin is, in fact, labeled at a unique site. Similar results were obtained previously with fluorescein isothiocyanate-labeled streptavidin (Blankenburg, R.; Meller, P.; Ringsdorf, H; Salesse, C. Biochemistry 1989, 28, 8214-8221.).
    • (1989) Biochemistry , vol.28 , pp. 8214-8221
    • Blankenburg, R.1    Meller, P.2    Ringsdorf, H.3    Salesse, C.4
  • 33
    • 1842291423 scopus 로고    scopus 로고
    • in press
    • Native, unbiotinylated lysozyme in the same concentration also disrupted streptavidin tiles. However, without biotin the process of crystal disruption was accompanied by a large increase in the surface pressure to >20 mN/m and required more than 45 min. Thus, disruption of streptavidin domains by native lysozyme appears to occur by a different mechanism. Most likely, lysozyme binds the IDA-Cu headgroups outside the streptavidin domains, increasing the surface pressure; lysozyme is known to have significant affinity for immobilized metal ions. The surface pressure increase could be responsible for the disappearance of protein from the interface (Vogel, V.; Schief Jr., W. R.; Frey, W. Supramol. Sci., in press).
    • Supramol. Sci.
    • Vogel, V.1    Schief Jr., W.R.2    Frey, W.3
  • 36
    • 1842408236 scopus 로고    scopus 로고
    • Ph.D. Thesis, California Institute of Technology
    • Pack, D. W. Ph.D. Thesis, California Institute of Technology, 1996.
    • (1996)
    • Pack, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.