[NMR paper] The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins
The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins
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...
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10-26-2022 07:20 AM
[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] An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.
An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.
An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.
J Am Chem Soc. 2017 Oct 09;:
Authors: Chien CH, Helfinger LR, Bostock MJ, Solt A, Tan YL, Nietlispach D
Abstract
Based on the saposin-A (SapA) scaffold protein we demonstrate the suitability of a size-adaptable phospholipid membrane-mimetic system for solution NMR studies of membrane proteins under close-to-native conditions. The Salipro...
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10-11-2017 10:37 AM
[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
Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs
Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs
Abstract
NMR structural studies on membrane proteins are often complicated by their large size, taking into account the contribution of the membrane mimetic. Therefore, classical resonance assignment approaches often fail. The large size of phospholipid nanodiscs, a detergent-free phospholipid bilayer mimetic, prevented their use in high-resolution solution-state NMR spectroscopy so far. We recently introduced smaller nanodiscs that are suitable for NMR...
Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR - Nature.com
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