Solid-state NMR is a quickly developing technique that allows one to obtain structural information at atomic resolution in extended lipid bilayers in a rather unique manner. Two approaches have been developed for membrane proteins and peptides namely magic angle sample spinning and the use of uniaxially oriented membrane samples. The state-of-the-art of both approaches will be introduced and the perspectives of solid-state NMR spectroscopy in the context of other structural biology techniques,...
[NMR paper] Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy
Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy
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...
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09-13-2022 11:49 AM
[NMR paper] High-Resolution Studies of Proteins in Natural Membranes by Solid-State NMR
High-Resolution Studies of Proteins in Natural Membranes by Solid-State NMR
Membrane proteins are vital for cell function and thus represent important drug targets. Solid-state Nuclear Magnetic Resonance (ssNMR) spectroscopy offers a unique access to probe the structure and dynamics of such proteins in biological membranes of increasing complexity. Here, we present modern solid-state NMR spectroscopy as a tool to study structure and dynamics of proteins in natural lipid membranes and at atomic scale. Such spectroscopic studies profit from the use of high-sensitivity...
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03-23-2021 07:56 PM
Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples #DNPNMR
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Salnikov, E.S., et al., Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples. ChemPhysChem, 2017. 18(15): p. 2103-2113.
https://www.ncbi.nlm.nih.gov/pubmed/28574169
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09-25-2017 08:42 PM
[NMR paper] Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.
Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.
J Magn Reson. 2015 Apr;253:50-9
Authors: Jaroniec CP
Abstract
Paramagnetism-based nuclear pseudocontact shifts and spin relaxation enhancements contain a wealth of information in solid-state NMR spectra about electron-nucleus distances on the ~20Å length...
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03-24-2015 09:58 PM
Structural studies of proteins by paramagnetic solid-state NMR spectroscopy
Structural studies of proteins by paramagnetic solid-state NMR spectroscopy
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Christopher P. Jaroniec</br>
Paramagnetism-based nuclear pseudocontact shifts and spin relaxation enhancements contain a wealth of information in solid-state NMR spectra about electron–nucleus distances on the ~20Å length scale, far beyond that normally probed through measurements of nuclear dipolar couplings. Such data are especially vital in the context of structural studies of proteins and other...
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03-20-2015 01:48 AM
[NMR paper] Temperature-Resistant Bicelles for Structural Studies by Solid-State NMR Spectroscopy.
Temperature-Resistant Bicelles for Structural Studies by Solid-State NMR Spectroscopy.
Temperature-Resistant Bicelles for Structural Studies by Solid-State NMR Spectroscopy.
Langmuir. 2015 Jan 7;
Authors: Yamamoto K, Pearcy P, Lee D, Yu C, Im S, Waskell LA, Ramamoorthy A
Abstract
Three-dimensional structure determination of membrane proteins is important to fully understand their biological functions. However, obtaining a high-resolution structure has been a major challenge mainly due to the difficulties in retaining the native...
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01-08-2015 01:29 PM
The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments.
The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments.
The structural and topological analysis of membrane-associated polypeptides by oriented solid-state NMR spectroscopy: Established concepts and novel developments.
Biophys Chem. 2010 Nov 12;
Authors: Bechinger B, Resende JM, Aisenbrey C
Solid-state NMR spectroscopy is a powerful technique for the investigation of membrane-associated peptides and proteins as well as their interactions with...
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12-15-2010 12:03 PM
[NMR paper] Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Related Articles Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Annu Rev Phys Chem. 2003;54:531-71
Authors: Drobny GP, Long JR, Karlsson T, Shaw W, Popham J, Oyler N, Bower P, Stringer J, Gregory D, Mehta M, Stayton PS
Proteins directly control the nucleation and growth of biominerals, but the details of molecular recognition at the protein-biomineral interface remain poorly understood. The elucidation of recognition...