[NMR paper] Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR
Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR
Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near-native lipid bilayer environment. The main limitation of the method is spectral resolution and sensitivity, however recent developments in ssNMR hardware, including the commercialization of 28...
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[NMR paper] Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.
Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.
Related Articles Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.
Biomol NMR Assign. 2020 Jun 30;:
Authors: Schubeis T, Schwarzer TS, Le Marchand T, Stanek J, Movellan KT, Castiglione K, Pintacuda G, Andreas LB
Abstract
Most commonly small outer membrane proteins, possessing between 8 and 12 ?-strands, are not involved in transport but fulfill diverse functions...
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07-02-2020 11:18 AM
NMR Structural Studies of the Yersinia Pestis Outer Membrane Protein AIL in Lipid Bilayers
NMR Structural Studies of the Yersinia Pestis Outer Membrane Protein AIL in Lipid Bilayers
Publication date: 2 February 2018
Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1</br>
Author(s): Yong Yao, Lynn Fujimoto, Samit Dutta, Francesca Marassi</br>
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02-07-2018 03:41 PM
[NMR paper] Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.
Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.
Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.
J Biomol NMR. 2015 Jan 13;
Authors: Ding Y, Fujimoto LM, Yao Y, Marassi FM
Abstract
Solid-state NMR studies of sedimented soluble proteins has been developed recently as an attractive approach for overcoming the size limitations of solution NMR spectroscopy while bypassing the...
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01-13-2015 02:31 PM
[NMR paper] Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Related Articles Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Chembiochem. 2014 Apr 1;
Authors: Sušac L, Horst R, Wüthrich K
Abstract
X-ray crystallography and solution NMR of detergent-reconstituted OmpA (outer membrane protein A from E. coli) had shown that this protein forms an eight-stranded transmembrane ?-barrel, but only...
Structure of outer membrane protein G in lipid bilayers - Nature.com
Linear Mode
