Related ArticlesInteractions of IDPs with Membranes Using Dark-State Exchange NMR Spectroscopy.
Methods Mol Biol. 2020;2141:585-608
Authors: Das T, Acosta D, Eliezer D
Abstract
Membrane interactions of proteins play a role in essential cellular processes in both physiological and disease states. The structural flexibility of intrinsically disordered proteins (IDPs) allows for interactions with multiple partners, including membranes. However, determining conformational states of IDPs when interacting with membranes can be challenging. Here we describe the use of nuclear magnetic resonance (NMR), including dark-state exchange saturation transfer (DEST), to probe IDP-membrane interactions in order to determine whether there is an interaction, which residues participate, and the extent/nature of the interaction between the protein and the membrane. Using ?-synuclein and tau as typical examples, we provide protocols for how the membrane interactions of IDPs can be probed, including details of how the samples should be prepared and guidelines on how to interpret the results.
[NMR paper] Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
J Struct Biol. 2017 Nov 29;:
Authors: Pinto C, Mance D, Julien M, Daniels M, Weingarth M, Baldus M
Abstract
Significant progress has been made in obtaining a structural insight into the assembly of the ?-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane...
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12-05-2017 07:35 PM
Depolarization of nuclear spin polarized 129Xe gas by dark rubidium during spin-exchange optical pumping
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Depolarization of nuclear spin polarized 129Xe gas by dark rubidium during spin-exchange optical pumping
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Antonacci, M.A., et al., Depolarization of nuclear spin polarized 129Xe gas by dark rubidium during spin-exchange optical pumping. J Magn Reson, 2017. 279: p. 60-67.
https://www.ncbi.nlm.nih.gov/pubmed/28475947
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08-23-2017 05:25 PM
[NMR paper] [Interactions between proteins and cation exchange adsorbents analyzed by NMR and hydrogen/deuterium exchange technique].
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Sheng Wu Gong Cheng Xue Bao. 2014 Sep;30(9):1454-63
Authors: Wang K, Hao D, Qi S, Ma G
Abstract
In silico acquirement of the accurate residue details of protein on chromatographic media is a bottleneck in protein chromatography separation and purification. Here we developed a novel approach by coupling with H/D exchange and nuclear magnetic resonance to observe hen egg white lysozyme (HEWL) unfolding behavior adsorbed on cation exchange media (SP Sepharose FF). Analysis of 1D 1H-NMR shows that protein unfolding accelerated...
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03-01-2015 12:18 PM
[NMR paper] Solid state NMR and protein-protein interactions in membranes.
Solid state NMR and protein-protein interactions in membranes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solid state NMR and protein-protein interactions in membranes.
Curr Opin Struct Biol. 2013 Sep 11;
Authors: Miao Y, Cross TA
Abstract
Solid state NMR spectroscopy has evolved rapidly in recent years into an excellent tool for the characterization of membrane proteins and their complexes. In the past few years it has also become clear that...
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09-17-2013 11:36 PM
Solid state NMR and protein–protein interactions in membranes
Solid state NMR and protein–protein interactions in membranes
Publication date: Available online 11 September 2013
Source:Current Opinion in Structural Biology</br>
Author(s): Yimin Miao , Timothy A Cross</br>
Solid state NMR spectroscopy has evolved rapidly in recent years into an excellent tool for the characterization of membrane proteins and their complexes. In the past few years it has also become clear that the structure of membrane proteins, especially helical membrane proteins is determined, in part, by the membrane environment. Therefore, the modeling of...
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09-11-2013 09:15 PM
[NMR paper] Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
Related Articles Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
Biochim Biophys Acta. 2013 Apr 5;
Authors: Ciesielski F, Griffin DC, Rittig M, Moriyón I, Bonev BB
Abstract
Lipopolysaccharide (LPS) is a major component of the external leaflet of bacterial outer membranes, key pro-inflammatory factor and an important mediator of host-pathogen interactions. In host cells it activates the complement...
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04-10-2013 07:21 PM
[NMR paper] Two-dimensional NMR spectroscopy reveals cation-triggered backbone degradation in polysulfone-based anion exchange membranes.
Two-dimensional NMR spectroscopy reveals cation-triggered backbone degradation in polysulfone-based anion exchange membranes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif Related Articles Two-dimensional NMR spectroscopy reveals cation-triggered backbone degradation in polysulfone-based anion exchange membranes.
Proc Natl Acad Sci U S A. 2013 Feb 12;110(7):2490-5
Authors: Arges CG, Ramani V
Abstract
Anion exchange membranes (AEMs) find...
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04-09-2013 06:31 PM
[NMR paper] The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.
Angew Chem Int Ed Engl. 2011 Aug 29;50(36):8432-5
Authors: Higman VA, Varga K, Aslimovska L, Judge PJ, Sperling LJ, Rienstra CM, Watts A
PMID: 21770003
Interactions of IDPs with Membranes Using Dark-State Exchange NMR Spectroscopy.
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