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  Insights into cholesterol/membrane protein interactions using paramagnetic solid-state NMR.

Jaipuria, G., Giller, K., Leonov, A., Becker, S., & Zweckstetter, M. (2018). Insights into cholesterol/membrane protein interactions using paramagnetic solid-state NMR. Chemistry - A European Journal, 24(66), 17606-17611. doi:10.1002/chem.201804550.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-47D7-C Version Permalink: http://hdl.handle.net/21.11116/0000-0003-6FED-7
Genre: Journal Article

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3001351.pdf (Publisher version), 2MB
 
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 Creators:
Jaipuria, G., Author
Giller, K.1, Author              
Leonov, A.1, Author              
Becker, S.1, Author              
Zweckstetter, M.2, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: NMR spectroscopy; lipid; membrane protein; protein structure
 Abstract: Cholesterol is an essential component of animal cell membranes and impacts the structure and function of membrane proteins. But how cholesterol exerts its functions remains often enigmatic. Here we show that high-resolution solid-state NMR in combination with paramagnetic cholesterol analogues is a powerful approach to study the interaction of membrane proteins with cholesterol. Application of the method to the 169-residue protein TSPO provides residue-specific information about its interaction with cholesterol. Comparison with NMR signal perturbations induced by diamagnetic cholesterol furthermore supports changes in the structure of mammalian TSPO caused by cholesterol binding.

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Language(s): eng - English
 Dates: 2018-09-252018-11-27
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/chem.201804550
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Title: Chemistry - A European Journal
Source Genre: Journal
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Pages: - Volume / Issue: 24 (66) Sequence Number: - Start / End Page: 17606 - 17611 Identifier: -