HACANCOi: a new H α -detected experiment for backbone resonance assignment of intrinsically disordered proteins
HACANCOi: a new H α -detected experiment for backbone resonance assignment of intrinsically disordered proteins
Abstract
Unidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T2) relaxation times allowing sophisticated coherence transfer pathway selection in comparison to folded proteins. 1Hα-detection ensures non-susceptibility to chemical exchange with the solvent and enables chemical shift assignment of consecutive proline residues,...
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10-29-2020 10:21 AM
[ASAP] Automated Backbone NMR Resonance Assignment of Large Proteins Using Redundant Linking from a Single Simultaneous Acquisition
Automated Backbone NMR Resonance Assignment of Large Proteins Using Redundant Linking from a Single Simultaneous Acquisition
Jan Stanek†‡#, Tobias Schubeis†#, Piotr Paluch‡, Peter Gu¨ntert??¶, Loren B. Andreas†§, and Guido Pintacuda*†
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c00251/20200316/images/medium/ja0c00251_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c00251
http://feeds.feedburner.com/~r/acs/jacsat/~4/VXpvMGcC9hY
[NMR paper] Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition.
Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition.
J Am Chem Soc. 2020 Mar 04;:
Authors: Stanek J, Schubeis T, Paluch P, Güntert P, Andreas LB, Pintacuda G
Abstract
Thanks to magic-angle spinning (MAS)...
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03-07-2020 06:20 PM
Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein
Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein
Abstract
New experiments dedicated for large IDPs backbone resonance assignment are presented. The most distinctive feature of all described techniques is the employment of MOCCA-XY16 mixing sequences to obtain effective magnetization transfers between carbonyl carbon backbone nuclei. The proposed 4 and 5 dimensional experiments provide a high dispersion of obtained signals making them suitable for use...
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07-20-2016 08:15 AM
[NMR paper] NMR Backbone Assignment of Large Proteins by Using (13) C? -Only Triple-Resonance Experiments.
NMR Backbone Assignment of Large Proteins by Using (13) C? -Only Triple-Resonance Experiments.
NMR Backbone Assignment of Large Proteins by Using (13) C? -Only Triple-Resonance Experiments.
Chemistry. 2016 Jun 8;
Authors: Wei Q, Chen J, Mi J, Zhang J, Ruan K, Wu J
Abstract
Nuclear magnetic resonance (NMR) is a powerful tool to interrogate protein structure and dynamics residue by residue. However, the prerequisite chemical-shift assignment remains a bottleneck for large proteins due to the fast relaxation and the frequency...
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06-09-2016 07:44 PM
[NMR paper] Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
Related Articles Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
J Struct Funct Genomics. 2014 Feb 18;
Authors: Reddy JG, Hosur RV
Abstract
Resonance assignment is the first and the most crucial step in all nuclear magnetic resonance (NMR) investigations on structure-function relationships in biological...
Mixed pyruvate labeling enables backbone resonance assignment of large proteins using a single experiment - Nature.com
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