Specific interactions with phospholipids are often critical for the function of proteins or drugs, but studying these interactions at high-resolution remains difficult, especially in complex membranes that mimic biological conditions. In principle, molecular interactions with phospholipids could be directly probed by solid-state NMR (ssNMR). However, due to the challenge to detect specific lipids in mixed liposomes and limited spectral sensitivity, ssNMR studies of specific lipids in complex...
[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
[NMR paper] High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.
High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.
Related Articles High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.
J Biomol NMR. 2017 Feb 26;:
Authors: Yao Y, Dutta SK, Park SH, Rai R, Fujimoto LM, Bobkov AA, Opella SJ, Marassi FM
Abstract
The outer membrane protein Ail (Adhesion invasion locus) is one of the most abundant proteins on the cell surface of Yersinia pestis during human infection. Its...
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02-28-2017 12:29 PM
High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes
High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes
Abstract
The outer membrane protein Ail (Adhesion invasion locus) is one of the most abundant proteins on the cell surface of Yersinia pestis during human infection. Its functions are expressed through interactions with a variety of human host proteins, and are essential for microbial virulence. Structures of Ail have been determined by X-ray diffraction and solution NMR spectroscopy, but those samples contained detergents that interfere...
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02-26-2017 08:27 PM
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
[NMR paper] Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Related Articles Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Biochim Biophys Acta. 2014 Jun 16;
Authors: Kinnun JJ, Mallikarjunaiah KJ, Petrache HI, Brown MF
Abstract
This article reviews the application of solid-state (2)H nuclear magnetic resonance (NMR) spectroscopy for investigating the deformation of lipid bilayers at the atomistic level. For...
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06-20-2014 08:14 PM
[NMR paper] The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State 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 G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
Chemistry. 2014 Mar 13;
Authors: Schmidt P, Thomas L, Müller P, Scheidt HA, Huster D
Abstract
Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy
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