Membrane Topology of an Ion Channel Detected by Solid-State Nuclear Magnetic Resonance and Paramagnetic Effects.

Autor:	Miao Y; Department of Chemistry, College of Staten Island-Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, New York 10016, United States., Lam D; Department of Chemistry, College of Staten Island-Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, New York 10016, United States., Zhuang J; Department of Chemistry, College of Staten Island-Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, New York 10016, United States., Zhu J; Department of Chemistry, College of Staten Island-Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, New York 10016, United States., Poget SF; Department of Chemistry, College of Staten Island-Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, New York 10016, United States., Tang M; Department of Chemistry, College of Staten Island-Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, New York 10016, United States.
Jazyk:	angličtina
Zdroj:	The journal of physical chemistry letters [J Phys Chem Lett] 2020 Nov 19; Vol. 11 (22), pp. 9795-9801. Date of Electronic Publication: 2020 Nov 05.
DOI:	10.1021/acs.jpclett.0c02014
Abstrakt:	Ion channels are often targeted by toxins or other ligands to modify their channel activities and alter ion conductance. Interactions between toxins and ion channels could result in changes in membrane insertion depth for residues close to the binding site. Paramagnetic solid-state nuclear magnetic resonance (SSNMR) has shown great potential in providing structural information on membrane samples. We used KcsA as a model ion channel to investigate how the paramagnetic effects of Mn 2+ and Dy 3+ ions with headgroup-modified chelator lipids would influence the SSNMR signals of membrane proteins in proteoliposomes. Spectral comparisons have shown significant changes of peak intensities for the residues in the loop or terminal regions due to paramagnetic effects corresponding to the close proximity to the membrane surface. Hence, these results demonstrate that paramagnetic SSNMR can be used to detect surface residues based on the topology and membrane insertion properties for integral membrane proteins.
Databáze:	MEDLINE
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