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Please use this identifier to cite or link to this item: http://elib.bsu.by/handle/123456789/49694
Title: Analysis of side chain rotational restrictions of membrane-embedded proteins by spin-label ESR spectroscopy
Authors: Strancar, J.
Kavalenka, A.
Ziherl, P.
Stopar, D.
Hemminga, M. A.
Keywords: ЭБ БГУ::ТЕХНИЧЕСКИЕ И ПРИКЛАДНЫЕ НАУКИ. ОТРАСЛИ ЭКОНОМИКИ::Электроника. Радиотехника
Issue Date: 2009
Publisher: Journal of Magnetic Resonance
Abstract: Site-directed spin-labeling electron spin resonance (SDSL-ESR) is a promising tool for membrane protein structure determination. Here we propose a novel way to translate the local structural constraints gained by SDSL-ESR data into a low-resolution structure of a protein by simulating the restrictions of the local conformational spaces of the spin label attached at different protein sites along the primary structure of the membrane-embedded protein. We test the sensitivity of this approach for membrane-embedded M13 major coat protein decorated with a limited number of strategically placed spin labels employing high-throughput site-directed mutagenesis. We find a reasonably good agreement of the simulated and the experimental data taking a protein conformation close to the one determined by fluorescence resonance energy transfer analysis [P.V. Nazarov, R.B.M. Koehorst, W.L. Vos, V.V. Apanasovich, M.A. Hemminga, FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein, Biophys. J. 92 (2007) 1296–1305].
URI: http://elib.bsu.by/handle/123456789/49694
Appears in Collections:Статьи факультета радиофизики и компьютерных технологий

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