Abstract
Lipid-nanodiscs have been shown to be an exciting innovation as a membrane-mimicking system for studies on membrane proteins by a variety of biophysical techniques, including NMR spectroscopy. Although NMR spectroscopy is unique in enabling the atomic-resolution investigation of dynamic structures of membrane-associated molecules, it, unfortunately, suffers from intrinsically low sensitivity. The long data acquisition often used to enhance the sensitivity is not desirable for sensitive membrane proteins. Instead, paramagnetic relaxation enhancement (PRE) has been used to reduce NMR data acquisition time or to reduce the amount of sample required to acquire an NMR spectra. However, the PRE approach involves the introduction of external paramagnetic probes in the system, which can induce undesired changes in the sample and on the observed NMR spectra. For example, the addition of paramagnetic ions, as frequently used, can denature the protein via direct interaction and also through sample heating. In this study, we show how the introduction of paramagnetic tags on the outer belt of polymer-nanodiscs can be used to speed-up data acquisition by significantly reducing the spin-lattice relaxation (T1) times with minimum-to-no alteration of the spectral quality. Our results also demonstrate the feasibility of using different types of paramagnetic ions (Eu3+, Gd3+, Dy3+, Er3+, Yb3+) for NMR studies on lipid-nanodiscs. Experimental results characterizing the formation of lipid-nanodiscs by the metal-chelated polymer, and their increased tolerance toward metal ions are also reported.
PMID: 32360741 [PubMed - as supplied by publisher]
[NMR paper] Exploring Lipid and Membrane Protein Dynamics Using Lipid-Bilayer Nanodiscs and Solution-State NMR Spectroscopy.
Exploring Lipid and Membrane Protein Dynamics Using Lipid-Bilayer Nanodiscs and Solution-State NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Exploring Lipid and Membrane Protein Dynamics Using Lipid-Bilayer Nanodiscs and Solution-State NMR Spectroscopy.
Methods Mol Biol. 2020;2127:397-419
Authors: Bibow S
Abstract
The relationship of membrane protein function and the surrounding lipid bilayer goes far beyond...
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03-03-2020 11:18 PM
[ASAP] Polymer Infiltration into Metal–Organic Frameworks in Mixed-Matrix Membranes Detected in Situ by NMR
Polymer Infiltration into Metal–Organic Frameworks in Mixed-Matrix Membranes Detected in Situ by NMR
Pu Duan, Jessica C. Moreton, Sergio R. Tavares, Rocio Semino, Guillaume Maurin, Seth M. Cohen, Klaus Schmidt-Rohr
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.9b02789/20190426/images/medium/ja-2019-02789g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.9b02789
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/nXRgCz-NW0I
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04-27-2019 09:18 PM
[NMR paper] Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins.
Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins.
Related Articles Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins.
J Biol Inorg Chem. 2017 Dec 07;:
Authors: Cerofolini L, Staderini T, Giuntini S, Ravera E, Fragai M, Parigi G, Pierattelli R, Luchinat C
Abstract
Paramagnetic NMR data can be profitably incorporated in structural refinement protocols of metalloproteins or metal-substituted proteins, mostly as distance or angle...
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12-10-2017 01:21 AM
[NMR paper] Gd(3+)-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins.
Gd(3+)-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins.
Related Articles Gd(3+)-chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins.
J Biomol NMR. 2017 May 30;:
Authors: Liu C, Liu J, Xu X, Xiang S, Wang S
Abstract
Solid-state NMR (SSNMR) is an attractive technique for studying large membrane proteins in membrane-mimetic environments. However, SSNMR experiments often suffer from low efficiency, due to the inherent low sensitivity and the long recycle...
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06-01-2017 03:02 PM
Gd 3+ -chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins
Gd 3+ -chelated lipid accelerates solid-state NMR spectroscopy of seven-transmembrane proteins
Abstract
Solid-state NMR (SSNMR) is an attractive technique for studying large membrane proteins in membrane-mimetic environments. However, SSNMR experiments often suffer from low efficiency, due to the inherent low sensitivity and the long recycle delays needed to recover the magnetization. Here we demonstrate that the incorporation of a small amount of a Gd3+-chelated lipid, Gd3+-DMPE-DTPA, into proteoliposomes greatly shortens the spinâ??lattice...
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[NMR paper] Shortening Spin-lattice Relaxation Using a Copper-Chelated lipid at Low-Temperatures – A Magic Angle Spinning Solid-State NMR Study on a Membrane-Bound Protein
Shortening Spin-lattice Relaxation Using a Copper-Chelated lipid at Low-Temperatures – A Magic Angle Spinning Solid-State NMR Study on a Membrane-Bound Protein
Publication date: Available online 1 November 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Kazutoshi Yamamoto , Marc Caporini , Sangchoul Im , Lucy Waskell , Ayyalusamy Ramamoorthy</br>
Inherent low sensitivity of NMR spectroscopy has been a major disadvantage, especially to study biomolecules like membrane proteins. Recent studies have successfully demonstrated the advantages of performing...
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
J Phys Chem B. 2011 Sep 22;
Authors: Yamamoto K, Vivekanandan S, Ramamoorthy A
Abstract
In spite of recent technological advances in NMR spectroscopy, its low sensitivity continues to be a major limitation particularly for the structural studies of membrane proteins. The need for a large quantity of a membrane protein and acquisition of...
Lipid-nanodiscs formed by paramagnetic metal chelated polymer for fast NMR data acquisition.
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