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  Absorption and fluorescence spectroscopic studies of the Ca2(+)-dependent lipid binding protein p36: the annexin repeat as the Ca2+ binding site.

Marriott, G., Kirk, W. R., Johnsson, N., & Weber, K. (1990). Absorption and fluorescence spectroscopic studies of the Ca2(+)-dependent lipid binding protein p36: the annexin repeat as the Ca2+ binding site. Biochemistry, 29(30), 7004-7011. doi:10.1021/bi00482a008.

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 Urheber:
Marriott, G.1, Autor           
Kirk, W. R., Autor
Johnsson, N.2, Autor           
Weber, K.2, Autor           
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society, ou_578618              

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 Zusammenfassung: The existence of a single tryptophan residue in the protein p36, a member of a recently characterized family of Ca2+ binding proteins called annexins, is exploited to provide unique spectroscopic information on the annexin repeat motif and its role in Ca2+ binding. The differences in ultraviolet absorption and fluorescence excitation upon Ca2+ binding are interpreted solely in terms of this tryptophan, which, in view of the pronounced blue-shifts and the presence of vibronic structure, seems to reside in a highly nonpolar environment. The fluorescence emission from the protein is correspondingly blue-shifted, and it is found to transfer energy in resonance with Tb3+ absorption lines in the near-ultraviolet. This effect allows us to locate the Tb3+ and, by implication, the Ca2+ binding site to within ca. 8 A of the tryptophan residue.

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Sprache(n): eng - English
 Datum: 1990-07-31
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1021/bi00482a008
ISI: A1990DR43700008
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Titel: Biochemistry
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 29 (30) Artikelnummer: - Start- / Endseite: 7004 - 7011 Identifikator: ISSN: 0006-2960