Related ArticlesSolid-state NMR triple-resonance backbone assignments in a protein.
J Biomol NMR. 1999 Apr;13(4):337-42
Authors: Tan WM, Gu Z, Zeri AC, Opella SJ
Triple-resonance solid-state NMR spectroscopy is demonstrated to sequentially assign the 13C' and 15N amide backbone resonances of adjacent residues in an oriented protein sample. The observed 13C' chemical shift frequency provides an orientational constraint complementary to those measured from the 1H and 15N amide resonances in double-resonance experiments.
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Abstract Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope labeling in conjunction with 15Nâ??1H correlation experiments. In this work an extended combinatorial selective in vitro labeling scheme is proposed that seeks to reduce the number of samples required for assignment. Including three...
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01-21-2012 06:26 PM
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Abstract The solution NMR resonance assignment of the protein backbone is most commonly carried out using triple resonance experiments that involve 15N and 1HN resonances. The assignment becomes problematic when there is resonance overlap of 15Nâ??1HN cross peaks. For such residues, one cannot unambiguously link the â??leftâ?? side of the NH root to the â??rightâ?? side, and the residues associated with such overlapping HN resonances remain often unassigned. Here we present a...
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12-31-2010 08:38 PM
[NMR paper] Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectro
Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
Related Articles Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
J Am Chem Soc. 2004 Sep 22;126(37):11422-3
Authors: Giraud N, Böckmann A, Lesage A, Penin F, Blackledge M, Emsley L
Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a...
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11-24-2010 10:01 PM
[NMR paper] Solid state NMR sequential resonance assignments and conformational analysis of the 2
Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.
Related Articles Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.
J Biomol NMR. 2003 Dec;27(4):323-39
Authors: Böckmann A, Lange A, Galinier A, Luca S, Giraud N, Juy M, Heise H, Montserret R, Penin F, Baldus M
Solid state NMR sample preparation and resonance assignments of the U- 2x10.4 kDa dimeric form...
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11-24-2010 09:16 PM
Automated protein resonance assignments of magic angle spinning solid-state NMR spect
Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of β1 immunoglobulin binding domain of protein G (GB1)
Abstract Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for proteins not amenable to other methods. However, few automated analysis tools are currently available for MAS SSNMR. We present a methodology for automating protein resonance assignments of MAS SSNMR spectral data and its application to experimental peak lists of the...
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10-15-2010 05:16 PM
Automated protein resonance assignments of magic angle spinning solid-state NMR spect
Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of ?1 immunoglobulin binding domain of protein G (GB1).
Related Articles Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of ?1 immunoglobulin binding domain of protein G (GB1).
J Biomol NMR. 2010 Oct 8;
Authors: Moseley HN, Sperling LJ, Rienstra CM
Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for...
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10-12-2010 02:52 PM
[NMR paper] Prospects for resonance assignments in multidimensional solid-state NMR spectra of un
Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins.
Related Articles Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins.
J Biomol NMR. 1996 Oct;8(3):239-51
Authors: Tycko R
The feasibility of assigning the backbone 15N and 13C NMR chemical shifts in multidimensional magic angle spinning NMR spectra of uniformly isotopically labeled proteins and peptides in unoriented solid samples is assessed by means of numerical simulations....
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08-22-2010 02:20 PM
[NMR paper] Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spe
Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy.
J Magn Reson. 1999 Jun;138(2):244-55
Authors: Krushelnitsky A, Reichert D, Hempel G, Fedotov V, Schneider H, Yagodina L, Schulga A
Superslow backbone dynamics of the protein barstar and the polypeptide polyglycine was studied by...
Solid-state NMR triple-resonance backbone assignments in a protein.
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