Related ArticlesA Suite of Solid-State NMR Experiments for RNA Intranucleotide Resonance Assignment in a 21 kDa Protein-RNA Complex.
Angew Chem Int Ed Engl. 2013 Jul 26;
Authors: Marchanka A, Simon B, Carlomagno T
Abstract
Intranucleotide resonance of the 26mer box C/D RNA in complex with the L7Ae protein were assigned by solid-state NMR (ssNMR; see picture) spectroscopy. This investigation opens the way for studying RNA in large protein-RNA complexes by ssNMR spectroscopy.
PMID: 23893717 [PubMed - as supplied by publisher]
[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
[NMR paper] Automated solid-state NMR resonance assignment of protein microcrystals and amyloids.
Automated solid-state NMR resonance assignment of protein microcrystals and amyloids.
Related Articles Automated solid-state NMR resonance assignment of protein microcrystals and amyloids.
J Biomol NMR. 2013 May 21;
Authors: Schmidt E, Gath J, Habenstein B, Ravotti F, Székely K, Huber M, Buchner L, Böckmann A, Meier BH, Güntert P
Abstract
Solid-state NMR is an emerging structure determination technique for crystalline and non-crystalline protein assemblies, e.g., amyloids. Resonance assignment constitutes the first and often very...
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05-22-2013 04:43 PM
[NMR paper] (13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
(13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
Related Articles (13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
Chemphyschem. 2013 Apr 15;
Authors: Barbet-Massin E, Pell AJ, Knight MJ, Webber AL, Felli IC, Pierattelli R, Emsley L, Lesage A, Pintacuda G
Abstract
We present two sequences which combine ((1) H,(15) N) and ((15) N,(13) C) selective cross-polarization steps with an efficient variant...
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04-17-2013 08:15 PM
[NMR paper] Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments
Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments
Available online 14 February 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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Structural measurements in magic-angle-spinning (MAS) solid-state NMR rely heavily on 13C-13C distance measurements. Broadbanded recoupling methods are used to generate many cross-peaks, but have complex polarization transfer mechanisms that limit the precision of distance constraints and can suffer from weak intensities for distant peaks due to relaxation, the...
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02-15-2013 05:21 PM
Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination
Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination
Abstract Several techniques for spectral editing of 2D 13Câ??13C correlation NMR of proteins are introduced. They greatly reduce the spectral overlap for five common amino acid types, thus simplifying spectral assignment and conformational analysis. The carboxyl (COO) signals of glutamate and aspartate are selected by suppressing the overlapping amide Nâ??CO peaks through 13Câ??15N dipolar dephasing. The sidechain methine (CH) signals of valine,...
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10-13-2012 04:42 AM
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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10-10-2011 06:27 AM
AUTOBA: Automation of backbone assignment from HN(C)N suite of experiments
AUTOBA: Automation of backbone assignment from HN(C)N suite of experiments
Abstract Development of efficient strategies and automation represent important milestones of progress in rapid structure determination efforts in proteomics research. In this context, we present here an efficient algorithm named as AUTOBA (Automatic Backbone Assignment) designed to automate the assignment protocol based on HN(C)N suite of experiments. Depending upon the spectral dispersion, the user can record 2D or 3D versions of the experiments for assignment. The algorithm uses as inputs: (i) protein primary...
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06-06-2011 12:53 AM
Suite of Six NMR Relaxation Dispersion Experiments to Study Multiple-Site Exchange in Proteins
http://pubs.acs.org/isubscribe/journals/jacsat/127/i44/figures/ja054550en00001.gif
Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments: An Application to the Folding of a Fyn SH3 Domain Mutant
Dmitry M. Korzhnev, Philipp Neudecker, Anthony Mittermaier, Vladislav Yu. Orekhov, and Lewis E. Kay*
Contribution from the Departments of Medical Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada, and Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden
J. Am. Chem....