Related ArticlesSolid-State NMR of Highly 13C-Enriched Cholesterol in Lipid Bilayers.
Methods. 2018 Jan 20;:
Authors: Della Ripa LA, Petros ZA, Cioffi AG, Piehl DW, Courtney JM, Burke MD, Rienstra CM
Abstract
Cholesterol (Chol) is vital for cell function as it is essential to a myriad of biochemical and biophysical processes. The atomistic details of Chol's interactions with phospholipids and proteins is therefore of fundamental interest, and NMR offers unique opportunities to interrogate these properties at high resolution. Towards this end, here we describe approaches for examining the structure and dynamics of Chol in lipid bilayers using high levels of 13C enrichment in combination with magic-angle spinning (MAS) methods. We quantify the incorporation levels and demonstrate high sensitivity and resolution in 2D 13C-13C and 1H-13C spectra, enabling de novo assignments and site-resolved order parameter measurements obtained in a fraction of the time required for experiments with natural abundance sterols. We envision many potential future applications of these methods to study sterol interactions with drugs, lipids and proteins.
PMID: 29366688 [PubMed - as supplied by publisher]
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR [Biophysics and Computational Biology]
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR
Matthew R. Elkins, Jonathan K. Williams, Martin D. Gelenter, Peng Dai, Byungsu Kwon, Ivan V. Sergeyev, Bradley L. Pentelute, Mei Hong...
Date: 2017-12-05
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol with M2, as with most eukaryotic membrane proteins, has long been elusive. We have now determined the cholesterol-binding site of... Read More
...
nmrlearner
Journal club
0
12-06-2017 08:02 AM
[NMR paper] Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Proc Natl Acad Sci U S A. 2017 Nov 20;:
Authors: Elkins MR, Williams JK, Gelenter MD, Dai P, Kwon B, Sergeyev IV, Pentelute BL, Hong M
Abstract
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol...
nmrlearner
Journal club
0
11-22-2017 02:01 PM
[NMR paper] Preparation of highly and generally enriched mammalian tissues for solid state NMR.
Preparation of highly and generally enriched mammalian tissues for solid state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Preparation of highly and generally enriched mammalian tissues for solid state NMR.
J Biomol NMR. 2015 Oct;63(2):119-23
Authors: Wong VW, Reid DG, Chow WY, Rajan R, Green M, Brooks RA, Duer MJ
Abstract
An appreciable level of isotope labelling is essential for future NMR structure elucidation of...
nmrlearner
Journal club
0
07-02-2016 07:23 PM
Preparation of highly and generally enriched mammalian tissues for solid state NMR
Preparation of highly and generally enriched mammalian tissues for solid state NMR
Abstract
An appreciable level of isotope labelling is essential for future NMR structure elucidation of mammalian biomaterials, which are either poorly expressed, or unexpressable, using micro-organisms. We present a detailed protocol for high level 13C enrichment even in slow turnover murine biomaterials (fur keratin), using a customized diet supplemented with commercial labelled algal hydrolysate and formulated as a gel to minimize wastage, which female mice...
nmrlearner
Journal club
0
09-26-2015 05:13 AM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
nmrlearner
Journal club
0
03-16-2011 04:15 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Jun Yang, Lubica Aslimovska and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109766n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/VmNlca5pCIw
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Biochemistry. 2010 Aug 30;
Authors: Kijac A, Shih AY, Nieuwkoop AJ, Schulten K, Sligar SG, Rienstra CM
Nanodiscs are an example of discoidal nanoscale lipid/protein particles that have been extremely useful for the biochemical and biophysical characterization of membrane proteins. They are discoidal lipid bilayer fragments encircled and stabilized by two amphipathic helical...