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Volumn 33, Issue 1, 1996, Pages 55-58

Excimer fluorescence to monitor transitions of the association-dissociation equilibria induced by dilution of proteins composed of subunits

Author keywords

Association; Conformation; Dilution; Excimer; Fluorescence; Subunit

Indexed keywords

ACTIN; PROTEIN; PROTEIN SUBUNIT;

EID: 0030588065     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0165-022X(96)00019-X     Document Type: Article
Times cited : (6)

References (10)
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  • 2
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    • Conformational drift and cryoinactivation of lactate dehydrogenase
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  • 3
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    • Dynamics and time-averaged chemical potential of proteins: Importance in oligomer association
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    • Xu, G.1    Weber, G.2
  • 4
    • 0023051838 scopus 로고
    • Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and hydrostatic pressure
    • [4] Weber, G., Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and hydrostatic pressure, Biochemistry, 25 (1986) 3626-3631.
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    • Weber, G.1
  • 5
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    • Dilution beyond a transition concentration and the enhanced filaments' formation of actin in the low ionic strength buffer
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    • (1995) Biochem. Mol. Biol. Intern. , vol.37 , pp. 1153-1161
    • Ikkai, T.1    Kondo, H.2
  • 6
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    • Exposure of actin thiols by the removal of tightly held calcium ions
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    • Fluorimetry study of N-(1-Pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
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  • 8
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    • Fluorescence spectroscopic studies of pyrene-actin adducts
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.