NMR spectroscopy provides structural and functional information about biomolecules and their complexes. The complexity of these systems can make the NMR data difficult to interpret, particularly for newer users of NMR technology, who may have limited understanding of the tools available and how they are used. To alleviate this problem, we have created software based on standardized workflows for both solution and solid-state NMR spectroscopy of proteins. These tools assist with manual and...
[NMR paper] Strategies for RNA Resonance Assignment by (13)C/(15)N- and (1)H-Detected Solid-State NMR Spectroscopy
Strategies for RNA Resonance Assignment by (13)C/(15)N- and (1)H-Detected Solid-State NMR Spectroscopy
Magic angle spinning (MAS) solid-state NMR (ssNMR) is an established tool that can be applied to non-soluble or non-crystalline biomolecules of any size or complexity. The ssNMR method advances rapidly due to technical improvements and the development of advanced isotope labeling schemes. While ssNMR has shown significant progress in structural studies of proteins, the number of RNA studies remains limited due to ssNMR methodology that is still underdeveloped. Resonance assignment is the...
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11-09-2021 10:05 AM
How to tackle protein structural data from solution and solid state: An integrated approach
How to tackle protein structural data from solution and solid state: An integrated approach
Publication date: February 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 92–93</br>
Author(s): Azzurra Carlon, Enrico Ravera, Witold Andra?oj?, Giacomo Parigi, Garib N. Murshudov, Claudio Luchinat</br>
Long-range NMR restraints, such as diamagnetic residual dipolar couplings and paramagnetic data, can be used to determine 3D structures of macromolecules. They are also used to monitor, and potentially to improve, the accuracy of a...
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04-09-2016 03:54 AM
[NMR paper] Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
Related Articles Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
J Biomol NMR. 2014 Sep 6;
Authors: Xiang S, Chevelkov V, Becker S, Lange A
Abstract
We introduce an efficient approach for sequential protein backbone assignment based on two complementary proton-detected 4D solid-state NMR experiments that correlate /Ni with CAi/COi or CAi-1/COi-1. The resulting 4D spectra exhibit excellent...
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09-07-2014 12:36 PM
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data
Abstract
We introduce an efficient approach for sequential protein backbone assignment based on two complementary proton-detected 4D solid-state NMR experiments that correlate \( {\text{H}}_{{\text{i}}}^{{\text{N}}} \) /Ni with CAi/COi or CAiâ??1/COiâ??1. The resulting 4D spectra exhibit excellent sensitivity and resolution and are amenable to (semi-)automatic assignment...
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09-06-2014 07:41 AM
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...
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12-06-2011 08:01 AM
A software framework for analysing solid-state MAS NMR data
A software framework for analysing solid-state MAS NMR data
Abstract Solid-state magic-angle-spinning (MAS) NMR of proteins has undergone many rapid methodological developments in recent years, enabling detailed studies of protein structure, function and dynamics. Software development, however, has not kept pace with these advances and data analysis is mostly performed using tools developed for solution NMR which do not directly address solid-state specific issues. Here we present additions to the CcpNmr Analysis software package which enable easier identification of spinning side...
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09-30-2011 08:01 PM
A software framework for analysing solid-state MAS NMR data.
A software framework for analysing solid-state MAS NMR data.
A software framework for analysing solid-state MAS NMR data.
J Biomol NMR. 2011 Sep 28;
Authors: Stevens TJ, Fogh RH, Boucher W, Higman VA, Eisenmenger F, Bardiaux B, van Rossum BJ, Oschkinat H, Laue ED
Abstract
Solid-state magic-angle-spinning (MAS) NMR of proteins has undergone many rapid methodological developments in recent years, enabling detailed studies of protein structure, function and dynamics. Software development, however, has not kept pace with these advances and...
nmrlearner
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09-30-2011 06:00 AM
A software framework for analysing solid-state MAS NMR data.
A software framework for analysing solid-state MAS NMR data.
A software framework for analysing solid-state MAS NMR data.
J Biomol NMR. 2011 Sep 28;
Authors: Stevens TJ, Fogh RH, Boucher W, Higman VA, Eisenmenger F, Bardiaux B, van Rossum BJ, Oschkinat H, Laue ED
Abstract
Solid-state magic-angle-spinning (MAS) NMR of proteins has undergone many rapid methodological developments in recent years, enabling detailed studies of protein structure, function and dynamics. Software development, however, has not kept pace with these advances...
POKY software tools encapsulating assignment strategies for solution and solid-state protein NMR data
Linear Mode
