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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.

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Marriott,  G.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Johnsson,  N.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Weber,  K.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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602947.pdf
(Publisher version), 948KB

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-0D7C-2
Abstract
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.