Membrane mimetics are essential for structural and functional studies of membrane proteins. A promising lipid-based system are phospholipid nanodiscs, where two copies of a so-called membrane scaffold protein (MSP) wrap around a patch of lipid bilayer. Consequently, the size of a nanodisc is determined by the length of the MSP. Furthermore, covalent MSP circularization was reported to improve nanodisc stability. However, a more detailed comparative analysis of the biophysical properties of...
[NMR paper] Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins
Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins
Membrane proteins (MPs) play essential roles in numerous cellular processes. Because around 70% of the currently marketed drugs target MPs, a detailed understanding of their structure, binding properties, and functional dynamics in a physiologically relevant environment is crucial for a more detailed understanding of this important protein class. We here summarize the benefits of using lipid nanodiscs for NMR structural investigations and provide a detailed overview of the currently used lipid...
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10-20-2021 06:28 AM
[NMR paper] Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.
Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.
Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.
Nat Protoc. 2018 Jan;13(1):79-98
Authors: Hagn F, Nasr ML, Wagner G
Abstract
Suitable membrane mimetics are crucial to the performance of structural and functional studies of membrane proteins. Phospholipid nanodiscs (formed when a membrane scaffold protein encircles a small portion of a lipid bilayer) have...
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12-08-2017 02:25 PM
[NMR paper] Optimizing nanodiscs and bicelles for solution NMR studies of two ?-barrel membrane proteins.
Optimizing nanodiscs and bicelles for solution NMR studies of two ?-barrel membrane proteins.
Related Articles Optimizing nanodiscs and bicelles for solution NMR studies of two ?-barrel membrane proteins.
J Biomol NMR. 2015 Apr;61(3-4):261-74
Authors: Kucharska I, Edrington TC, Liang B, Tamm LK
Abstract
Solution NMR spectroscopy has become a robust method to determine structures and explore the dynamics of integral membrane proteins. The vast majority of previous studies on membrane proteins by solution NMR have been conducted in...
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04-15-2015 04:40 PM
Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins
Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins
Abstract
Solution NMR spectroscopy has become a robust method to determine structures and explore the dynamics of integral membrane proteins. The vast majority of previous studies on membrane proteins by solution NMR have been conducted in lipid micelles. Contrary to the lipids that form a lipid bilayer in biological membranes, micellar lipids typically contain only a single hydrocarbon chain or two chains that are too short to form a bilayer. Therefore,...
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02-10-2015 10:56 AM
Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature
From The DNP-NMR Blog:
Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature
Solid-state DNP-NMR are typically performed at cryogenic temperatures and samples, especially bio-macromolecules often require cryo-protection. This is a recent review about sample preparation and cryo-protecting samples to preserve the spectral resolution.
Lee, M. and M. Hong, Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature. J Biomol NMR, 2014....
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08-27-2014 02:29 PM
[NMR paper] Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature.
Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature.
Related Articles Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature.
J Biomol NMR. 2014 Jul 12;
Authors: Lee M, Hong M
Abstract
Solid-state NMR spectra of membrane proteins often show significant line broadening at cryogenic temperatures. Here we investigate the effects of several cryoprotectants to preserve the...
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07-13-2014 06:48 PM
Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature
Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature
Abstract
Solid-state NMR spectra of membrane proteins often show significant line broadening at cryogenic temperatures. Here we investigate the effects of several cryoprotectants to preserve the spectral resolution of lipid membranes and membrane peptides at temperatures down to ~200Â*K. Trehalose, glycerol, dimethylsulfoxide (DMSO), dimethylformamide (DMF), and polyethylene glycol (PEG), were chosen. These compounds are...
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07-12-2014 06:07 PM
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
Bioorg Chem. 2011 Feb;39(1):59-66
Authors: Borioni A, Bastanzio G, Delfini M, Mustazza C, Sciubba F, Tatti M, Del Giudice MR
The interaction of new bivalent NOP receptor antagonists with dodecyl phosphatidylcholine micelles and DMPC/cholesterol liposomes was investigated in solution by high resolution NMR. The ligands are...
The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins
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