Publication date: Available online 25 April 2018 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Victoria A. Higman
The prerequisite to structural or functional studies of proteins by NMR is generally the assignment of resonances. Since the first assignment of proteins by solid-state MAS NMR was conducted almost two decades ago, a wide variety of different pulse sequences and methods have been proposed and continue to be developed. Traditionally, a variety of 2D and 3D 13C-detected experiments have been used for the assignment of backbone and side-chain 13C and 15N resonances. These methods have found widespread use across the field. But as the hardware has changed and higher spinning frequencies and magnetic fields are becoming available, the ability to use direct proton detection is opening up a new set of assignment methods based on triple-resonance experiments. This review describes solid-state MAS NMR assignment methods using carbon detection and proton detection at different deuteration levels. The use of different isotopic labelling schemes as an aid to assignment in difficult cases is discussed as well as the increasing number of software packages that support manual and automated resonance assignment. Graphical abstract
[NMR paper] Solid-state NMR H-N-(C)-H and H-N-C-C 3D/4D correlation experiments for resonance assignment of large proteins.
Solid-state NMR H-N-(C)-H and H-N-C-C 3D/4D correlation experiments for resonance assignment of large proteins.
Related Articles Solid-state NMR H-N-(C)-H and H-N-C-C 3D/4D correlation experiments for resonance assignment of large proteins.
Chemphyschem. 2017 Aug 09;:
Authors: Fraga H, Arnaud CA, Gauto DF, Audin MJC, Kurauskas V, Macek P, Krichel C, Guan JY, Boisbouvier J, Sprangers R, Breyton C, Schanda P
Abstract
Solid-state NMR can provide insight into protein structure and dynamics at the atomic level without inherent protein...
nmrlearner
Journal club
0
08-10-2017 01:27 PM
[NMR paper] Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Proton-Detected NMR Spectroscopy of Nanodisc-Embedded Membrane Proteins: MAS Solid-State vs. Solution-State Methods.
J Phys Chem B. 2017 Jul 24;:
Authors: Lakomek NA, Frey L, Bibow S, Böckmann A, Riek R, Meier BH
Abstract
The structural and dynamical characterization of membrane proteins...
nmrlearner
Journal club
0
07-25-2017 07:46 PM
[NMR paper] Solid-state NMR methods for oriented membrane proteins.
Solid-state NMR methods for oriented membrane proteins.
Related Articles Solid-state NMR methods for oriented membrane proteins.
Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:48-85
Authors: Hansen SK, Bertelsen K, Paaske B, Nielsen NC, Vosegaard T
Abstract
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...
nmrlearner
Journal club
0
08-19-2015 03:24 PM
Solid-state NMR methods for oriented membrane proteins
From The DNP-NMR Blog:
Solid-state NMR methods for oriented membrane proteins
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.
nmrlearner
News from NMR blogs
0
08-04-2015 01:43 AM
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...
nmrlearner
Journal club
0
05-19-2015 09:10 AM
[NMR paper] BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.
BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.
Related Articles BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.
J Biomol NMR. 2014 Mar 1;
Authors: Shi C, Fasshuber HK, Chevelkov V, Xiang S, Habenstein B, Vasa SK, Becker S, Lange A
Abstract
We have recently presented band-selective homonuclear cross-polarization (BSH-CP) as an efficient method for CO-CA transfer in deuterated as well as protonated solid proteins. Here we show how the BSH-CP CO-CA transfer block can be incorporated...
nmrlearner
Journal club
0
03-04-2014 06:37 PM
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins
Abstract Biological solid-state nuclear magnetic resonance spectroscopy developed rapidly in the past two decades and emerged as an important tool for structural biology. Resonance assignment is an essential prerequisite for structure determination and the characterization of motional properties of a molecule. Experiments, which rely on carbon or nitrogen detection, suffer, however, from low sensitivity. Recently, we introduced the RAP (Reduced Adjoining Protonation) labeling scheme, which...
nmrlearner
Journal club
0
12-06-2011 08:01 AM
[NMR paper] Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional
Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR.
Related Articles Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR.
J Biomol NMR. 1999 Sep;15(1):1-14
Authors: Hong M
The comprehensive structure determination of isotopically labeled proteins by solid-state NMR requires sequence-specific assignment of 13C and 15N spectra. We describe several 2D and 3D MAS correlation techniques for resonance assignment and apply them, at 7.0...
Solid-state MAS NMR resonance assignment methods for proteins
Linear Mode
