¹H-detected solid-state NMR spectroscopy has been becoming increasingly popular for the characterization of protein structure, dynamics, and function. Recently, we showed that higher-dimensionality solid-state NMR spectroscopy can aid resonance assignments in large micro-crystalline protein targets to combat ambiguity (Klein et al., Proc. Natl. Acad. Sci. U.S.A. 2022). However, assignments represent both, a time-limiting factor and one of the major practical disadvantages within solid-state NMR...
5D solid-state NMR spectroscopy for facilitated resonance assignment
5D solid-state NMR spectroscopy for facilitated resonance assignment
Abstract
1H-detected solid-state NMR spectroscopy has been becoming increasingly popular for the characterization of protein structure, dynamics, and function. Recently, we showed that higher-dimensionality solid-state NMR spectroscopy can aid resonance assignments in large micro-crystalline protein targets to combat ambiguity (Klein et al., Proc. Natl. Acad. Sci. U.S.A. 2022). However, assignments represent both, a time-limiting factor and one of the major practical disadvantages...
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11-10-2023 12:26 AM
Protein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS
Protein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS
Abstract
Solid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (1H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of 1H-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) 13C spectroscopy,...
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11-24-2021 09:01 PM
[NMR paper] Protein resonance assignment by solid-state NMR based on (1)H-detected (13)C double-quantum spectroscopy at fast MAS
Protein resonance assignment by solid-state NMR based on (1)H-detected (13)C double-quantum spectroscopy at fast MAS
Solid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (¹H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of ¹H-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) ^(13)C spectroscopy, detected on ¹H, is proposed for fast MAS...
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11-24-2021 06:01 AM
[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
[NMR paper] Solid-state MAS NMR resonance assignment methods for proteins.
Solid-state MAS NMR resonance assignment methods for proteins.
Related Articles Solid-state MAS NMR resonance assignment methods for proteins.
Prog Nucl Magn Reson Spectrosc. 2018 Jun - Aug;106-107:37-65
Authors: Higman VA
Abstract
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...
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05-06-2019 04:47 PM
Solid-state MAS NMR resonance assignment methods for proteins
Solid-state MAS NMR resonance assignment methods for proteins
Publication date: Available online 25 April 2018
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Victoria A. Higman</br>
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...
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04-26-2018 02:15 AM
Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment
Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment
Abstract
Magic-angle spinning solid-state NMR has been applied to study CBM3bâ??Cbh9A (CBM3b), a cellulose binding module protein belonging to family 3b. It is a 146-residue protein having a unique nine-stranded β-sandwich fold, in which 35Â*% of the structure is in a β-sheet conformation and the remainder of the protein is composed of loops and unstructured regions. Yet, the protein can be crystalized...
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06-19-2014 10:21 PM
[NMR paper] Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.
Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.
J Biomol NMR. 2014 May 14;
Authors: Ivanir H, Goldbourt A
Abstract
Magic-angle spinning...
5D solid-state NMR spectroscopy for facilitated resonance assignment
Linear Mode
