Related ArticlesTowards 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 [Formula: see text]/Ni with CAi/COi or CAi-1/COi-1. The resulting 4D spectra exhibit excellent sensitivity and resolution and are amenable to (semi-)automatic assignment approaches. This strategy allows to obtain sequential connections with high confidence as problems related to peak overlap and multiple assignment possibilities are avoided. Non-uniform sampling schemes were implemented to allow for the acquisition of 4D spectra within a few days. Rather moderate hardware requirements enable the successful demonstration of the method on deuterated type III secretion needles using a 600 MHz spectrometer at a spinning rate of 25 kHz.
PMID: 25193427 [PubMed - as supplied by publisher]
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
[NMR paper] Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.
Related Articles Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins.
J Magn Reson. 2014 Mar 4;242C:180-188
Authors: Chevelkov V, Habenstein B, Loquet A, Giller K, Becker S, Lange A
Abstract
Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system...
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03-29-2014 01:00 PM
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins
Proton-detected MAS NMR experiments based on dipolar transfers for backbone assignment of highly deuterated proteins
Publication date: Available online 4 March 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Veniamin Chevelkov , Birgit Habenstein , Antoine Loquet , Karin Giller , Stefan Becker , Adam Lange</br>
Proton-detected solid-state NMR was applied to a highly deuterated insoluble, non-crystalline biological assembly, the Salmonella typhimurium type iii secretion system (T3SS) needle. Spectra of very high resolution and sensitivity were obtained...
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03-04-2014 06:37 PM
[NMR paper] Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.
Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.
Related Articles Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.
J Biomol NMR. 2013 Jun 29;
Authors: Barbet-Massin E, Pell AJ, Jaudzems K, Franks WT, Retel JS, Kotelovica S, Akopjana I, Tars K, Emsley L, Oschkinat H, Lesage A, Pintacuda G
Abstract
We present here (1)H-detected triple-resonance H/N/C experiments that...
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07-03-2013 01:46 PM
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Abstract Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the...
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09-20-2012 06:06 AM
Proton-Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin
Proton-Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin
Meaghan E. Ward, Lichi Shi, Evelyn Lake, Sridevi Krishnamurthy, Howard Hutchins, Leonid S. Brown and Vladimir Ladizhansky
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207137h/aop/images/medium/ja-2011-07137h_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207137h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Vzwkh1cjxOU
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10-09-2011 06:15 AM
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
J Am Chem Soc. 2011 Sep 16;
Authors: Ward ME, Shi L, Lake EM, Krishnamurthy S, Hutchins H, Brown LS, Ladizhansky V
Abstract
We used high-resolution proton-detected multidimensional NMR to study the solvent-exposed parts of an integral seven-helical membrane proton pump proteorhodopsin...
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09-17-2011 08:21 PM
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
Chemphyschem. 2011 Apr 4;12(5):915-8
Authors: Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH