Solid-state NMR (ssNMR) spectroscopy has emerged as the method of choice to analyze the structural dynamics of fibrillar, membrane-bound, and crystalline proteins that are recalcitrant to other structural techniques. Recently, 1 H detection under fast magic angle spinning and multiple acquisitions ssNMR techniques have propelled the structural analysis of complex biomacromolecules. However, data acquisition and resonance-specific assignments remain a bottleneck for this technique. Here, we...
[NMR paper] Identification of RNA base pairs and complete assignment of nucleobase resonances by 1H-detected solid-state NMR spectroscopy at 100 kHz MAS
Identification of RNA base pairs and complete assignment of nucleobase resonances by 1H-detected solid-state NMR spectroscopy at 100 kHz MAS
Knowledge of RNA structure, either in isolation or in complex, is fundamental to understand the mechanism of cellular processes. Solid-state NMR (ssNMR) is applicable to high molecular-weight complexes and does not require crystallization; thus, it is well-suited to study RNA as part of large multicomponent assemblies. Recently, we solved the first structures of both RNA and an RNA-protein complex by ssNMR using conventional 13 C- and 15 N-detection....
nmrlearner
Journal club
0
08-12-2021 08:56 AM
[NMR paper] Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Related Articles Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
J Biomol NMR. 2016 Jan 19;
Authors: Wang S, Matsuda I, Long F, Ishii Y
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce...
nmrlearner
Journal club
0
01-20-2016 11:54 PM
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce the ambiguity for protein main-chain signal assignments in fast magic-angle-spinning (MAS) conditions at a wide frequency range of 40â??80Â*kHz. The approach termed HIGHLIGHT (Wang et al., in Chem Comm 51:15055â??15058, 2015) combines the reverse 13C,...
nmrlearner
Journal club
0
01-19-2016 07:37 PM
Automated robust and accurate assignment of protein resonances for solid state NMR
Automated robust and accurate assignment of protein resonances for solid state NMR
Abstract
The process of resonance assignment represents a time-consuming and potentially error-prone bottleneck in structural studies of proteins by solid-state NMR (ssNMR). Software for the automation of this process is therefore of high interest. Procedures developed through the last decades for solution-state NMR are not directly applicable for ssNMR due to the inherently lower data quality caused by lower sensitivity and broader lines, leading to overlap between...
nmrlearner
Journal club
0
06-19-2014 10:21 PM
[NMR paper] Automated robust and accurate assignment of protein resonances for solid state NMR.
Automated robust and accurate assignment of protein resonances for solid state NMR.
Automated robust and accurate assignment of protein resonances for solid state NMR.
J Biomol NMR. 2014 May 10;
Authors: Nielsen JT, Kulminskaya N, Bjerring M, Nielsen NC
Abstract
The process of resonance assignment represents a time-consuming and potentially error-prone bottleneck in structural studies of proteins by solid-state NMR (ssNMR). Software for the automation of this process is therefore of high interest. Procedures developed through...
nmrlearner
Journal club
0
05-13-2014 03:11 PM
[NMR paper] Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human cal
Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy.
Related Articles Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy.
Protein Sci. 1998 Nov;7(11):2421-30
Authors: Qian H, Rogers MS, Schleucher J, Edlund U, Strehler EE, Sethson I
Human calmodulin-like protein (CLP) is closely related to vertebrate calmodulin, yet its unique cell specific expression pattern, overlapping but...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by
Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
Related Articles Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
J Biomol NMR. 1996 Dec;8(4):417-28
Authors: Sethson I, Edlund U, Holak TA, Ross A, Jonsson BH
The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of...
PHRONESIS: a one-shot approach for sequential assignment of protein resonances by ultrafast MAS solid-state NMR spectroscopy
Linear Mode
