This review article gives a comprehensive overview of the field of solid-state NMR spectroscopy on oriented samples. These experiments are typically less demanding on instrumentation since experiments are performed on static samples, without the need of spinning. While this article is not directly related to DNP-NMR spectroscopy, DNP-NMR on static samples will certainly become more interesting in the future.
Hansen, S.K., et al., Solid-state NMR methods for oriented membrane proteins. Prog. NMR. Spec., 2015. 88-89: p. 48-85.
Oriented-sample solid-state NMR represents one of few experimental methods capable of characterising the membrane-bound conformation of proteins in the cell membrane. Since the technique was developed 25 years ago, the technique has been applied to study the structure of helix bundle membrane proteins and antimicrobial peptides, characterise protein-lipid interactions, and derive information on dynamics of the membrane anchoring of membrane proteins. We will review the major developments in various aspects of oriented-sample solid-state NMR, including sample-preparation methods, pulse sequences, theory required to interpret the experiments, perspectives for and guidelines to new experiments, and a number of representative applications.
Solid-State NMR Methods for Oriented Membrane Proteins
Solid-State NMR Methods for Oriented Membrane Proteins
Publication date: Available online 19 May 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Sara K. Hansen , Kresten Bertelsen , Berit Paaske , Niels Chr. Nielsen , Thomas Vosegaard</br>
Oriented-sample solid-state NMR represents one of few experimental methods capable of characterising the membrane-bound conformation of proteins in the cell membrane. Since the technique was developed 25 years ago, the technique has been applied to study the structure of helix bundle membrane...
[NMR paper] Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins.
Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins.
Related Articles Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins.
Prog Nucl Magn Reson Spectrosc. 2013 Nov;75:50-68
Authors: Gopinath T, Mote KR, Veglia G
Abstract
Oriented solid-state NMR (O-ssNMR) spectroscopy is a major technique for the high-resolution analysis of the structure and topology of transmembrane proteins in native-like environments. Unlike magic angle spinning (MAS)...
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[NMR paper] Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Related Articles Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Nat Protoc. 2013 Nov;8(11):2256-70
Authors: Das N, Murray DT, Cross TA
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Sensitivity and Resolution Enhancement of Oriented Solid-State NMR: Application to Membrane Proteins
Sensitivity and Resolution Enhancement of Oriented Solid-State NMR: Application to Membrane Proteins
Publication date: Available online 12 August 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): T. Gopinath , Kaustubh R. Mote , Gianluigi Veglia</br>
Oriented solid-state NMR (O-ssNMR) spectroscopy is a major technique for the high-resolution analysis of the structure and topology of transmembrane proteins in native-like environments. Unlike magic angle spinning (MAS) techniques, O-ssNMR spectroscopy requires membrane protein...
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...