Solid-state nuclear magnetic resonance (ssNMR) methods can probe the motions of membrane proteins in liposomes at the atomic level and propel the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. In this work, we report our study on the fluoride channel Fluc-Ec1 in phospholipid bilayers based on ssNMR and molecular dynamics simulations. Previously unidentified fluoride binding sites in the aqueous vestibules were experimentally...
[NMR paper] Structural Mechanism of Soluble N-ethylmaleimide-Sensitive Factor Attachment Protein Receptor Complex Assembly in Lipid Bilayers Revealed by Solid-State NMR
Structural Mechanism of Soluble N-ethylmaleimide-Sensitive Factor Attachment Protein Receptor Complex Assembly in Lipid Bilayers Revealed by Solid-State NMR
Synaptic vesicle fusion is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, including synaptobrevin-2 (Syb-2), syntaxin-1 (Syx-1), and SNAP-25. However, it remains controversial whether the formation of thoroughly contacted ?-helical bundle from the SNARE motifs to the end of the transmembrane domains (TMDs) is necessary for SNARE-mediated membrane fusion. In this study, we...
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[NMR paper] Solid-state NMR study of structural heterogeneity of the apo WT mouse TSPO reconstituted in liposomes
Solid-state NMR study of structural heterogeneity of the apo WT mouse TSPO reconstituted in liposomes
In the last decades, ligand binding to human TSPO has been largely used in clinical neuroimaging, but little is known about the interaction mechanism. Protein conformational mobility plays a key role in the ligand recognition and both, ligand-free and ligand-bound structures, are mandatory for characterizing the molecular binding mechanism. In the absence of crystals for mammalian TSPO, we have exploited solid-state nuclear magnetic resonance (ssNMR) spectroscopy under magic-angle spinning...
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[ASAP] Gating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-State NMR Spectroscopy
Gating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-State NMR Spectroscopy
Yongxiang Zhao, Huayong Xie, Lili Wang, Yang Shen, Wei Chen, Benteng Song, Zhengfeng Zhang, Anmin Zheng, Qingsong Lin, Riqiang Fu, Jufang Wang, Jun Yang
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b03446/20180611/images/medium/ja-2018-03446h_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b03446
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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[NMR paper] Gating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-state NMR Spectroscopy.
Gating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-state NMR Spectroscopy.
Related Articles Gating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-state NMR Spectroscopy.
J Am Chem Soc. 2018 May 25;:
Authors: Zhao Y, Xie H, Wang L, Shen Y, Chen W, Song B, Zhang Z, Zheng A, Lin Q, Fu R, Wang J, Yang J
Abstract
Aquaporin Z (AqpZ) is an integral membrane protein that facilitates transport of water across E. coli cells with a high rate. Previously, R189,...
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Detergent Optimized Membrane Protein Reconstitutionin Liposomes for Solid State NMR
Detergent Optimized Membrane Protein Reconstitutionin Liposomes for Solid State NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500144h/aop/images/medium/bi-2014-00144h_0008.gif
Biochemistry
DOI: 10.1021/bi500144h
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/hfZQKdLVNh4
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[NMR paper] Detergent Optimized Membrane Protein Reconstitution in Liposomes for Solid State NMR.
Detergent Optimized Membrane Protein Reconstitution in Liposomes for Solid State NMR.
Related Articles Detergent Optimized Membrane Protein Reconstitution in Liposomes for Solid State NMR.
Biochemistry. 2014 Mar 25;
Authors: Murray DT, Griffin JM, Cross TA
Abstract
For small helical membrane proteins their structure is highly sensitive to their environment and solid state NMR is a structural technique that can characterize these membrane proteins in native like lipid bilayers and proteoliposomes. To date, a systematic method by which to...
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[NMR paper] The mechanism of aluminum-independent G-protein activation by fluoride and magnesium.
The mechanism of aluminum-independent G-protein activation by fluoride and magnesium. 31P NMR spectroscopy and fluorescence kinetic studies.
Related Articles The mechanism of aluminum-independent G-protein activation by fluoride and magnesium. 31P NMR spectroscopy and fluorescence kinetic studies.
J Biol Chem. 1993 Feb 5;268(4):2393-402
Authors: Antonny B, Sukumar M, Bigay J, Chabre M, Higashijima T
With magnesium present, fluoride and aluminum ions activate heterotrimeric G-proteins by forming AlFx complexes that mimic the gamma phosphate of...
Fluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR
Linear Mode
