The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
3D TEDOR NMR Experiments for the Simultaneous Measurement of Multiple Carbon−Nitrogen Distances in Uniformly13C,15N-Labeled Solids
Abstract
We describe three-dimensional magic-angle-spinning NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C,(15)N-labeled solids. The approaches employ transferred echo double resonance (TEDOR) for (13)C-(15)N coherence transfer and (15)N and (13)C frequency labeling for site-specific resolution, and build on several previous 3D TEDOR techniques. The novel feature of the 3D TEDOR pulse sequences presented here is that they are specifically designed to circumvent the detrimental effects of homonuclear (13)C-(13)C J-couplings on the measurement of weak (13)C-(15)N dipolar couplings. In particular, homonuclear J-couplings lead to two undesirable effects: (i) they generate anti-phase and multiple-quantum (MQ) spin coherences, which lead to spurious cross-peaks and phase-twisted lines in the 2D (15)N-(13)C correlation spectra, and thus degrade the spectral resolution and prohibit the extraction of reliable cross-peak intensities, and (ii) they significantly reduce cross-peak intensities for strongly J-coupled (13)C sites (e.g., CO and C(alpha)). The first experiment employs z-filter periods to suppress the anti-phase and MQ coherences and generates 2D spectra with purely absorptive peaks for all TEDOR mixing times. The second approach uses band-selective (13)C pulses to refocus J-couplings between (13)C spins within the selective pulse bandwidth and (13)C spins outside the bandwidth. The internuclear distances are extracted by using a simple analytical model, which accounts explicitly for multiple spin-spin couplings contributing to cross-peak buildup. The experiments are demonstrated in two U-(13)C,(15)N-labeled peptides, N-acetyl-L-Val-L-Leu (N-ac-VL) and N-formyl-L-Met-L-Leu-L-Phe (N-f-MLF), where 20 and 26 (13)C-(15)N distances up to approximately 5-6 A were measured, respectively. Of the measured distances, 10 in N-ac-VL and 13 in N-f-MLF are greater than 3 A and provide valuable structural constraints.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Principles of Nuclear Magnetic Resonance in One and Two Dimensions
Ernst, R. R., Bodenhausen, G., Wokaun, A., & Redfield, A. G. (1989) · Physics Today · doi:10.1063/1.2811094 · Cited by 4,201
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
Enhancement of nuclear magnetic resonance signals by polarization transfer
Morris, G. A., & Freeman, R. (1979) · Journal of the American Chemical Society · doi:10.1021/ja00497a058 · Cited by 2,015
Protein NMR Spectroscopy: Principles and Practice
Cavanagh, J. (1995) · Cited by 1,636
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,628
Principles of Nuclear Magnetic Resonance in One and Two Dimensions
Ernst, R. R., Bodenhausen, G., & Wokaun, A. (1990) · doi:10.1093/oso/9780198556473.001.0001 · Cited by 1,418
Ramped-Amplitude Cross Polarization in Magic-Angle-Spinning NMR
Metz, G., Wu, X. L., & Smith, S. O. (1994) · Journal of Magnetic Resonance, Series A · doi:10.1006/jmra.1994.1208 · Cited by 1,217
Spera, S., & Bax, A. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00014a071 · Cited by 1,087
Protein NMR Spectroscopy. Principles and Practice
Kalbitzer, H. R. (1997) · Zeitschrift für Physikalische Chemie · doi:10.1524/zpch.1997.202.part_1_2.297 · Cited by 971
High Resolution Nmr in Solids Selective Averaging
(1976) · Elsevier eBooks · doi:10.1016/b978-0-12-025561-0.x5001-1 · Cited by 825
Cited by
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Paravastu, A. K., Leapman, R. D., Yau, W.-M., & Tycko, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806270105 · Cited by 1,160
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
Atomic structure and hierarchical assembly of a cross-β amyloid fibril
Fitzpatrick, A. W. P., Debelouchina, G. T., Bayro, M. J., Clare, D. K., Caporini, M. A., Bajaj, V. S., Jaroniec, C. P., Wang, L., Ladizhansky, V., Müller, S. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219476110 · Cited by 565
Self-citationMolecular structure of amyloid fibrils: insights from solid-state NMR
Tycko, R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004173 · Cited by 527
Nmrglue: an open source Python package for the analysis of multidimensional NMR data
Helmus, J. J., & Jaroniec, C. P. (2013) · Journal of Biomolecular NMR · doi:10.1007/s10858-013-9718-x · Cited by 383
Self-citationMolecular architecture of fungal cell walls revealed by solid-state NMR
Kang, X., Kirui, A., Muszyński, A., Widanage, M. C. D., Chen, A., Azadi, P., Wang, P., Mentink-Vigier, F., & Wang, T. (2018) · Nature Communications · doi:10.1038/s41467-018-05199-0 · Cited by 356
Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR
McDermott, A. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133719 · Cited by 342
The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., & McDermott, A. E. (2018) · Cell · doi:10.1016/j.cell.2018.03.032 · Cited by 336
Li, S., & Hong, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja108943n · Cited by 296
Schanda, P., & Ernst, M. (2016) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2016.02.001 · Cited by 264
Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril
Jaroniec, C. P., MacPhee, C. E., Astrof, N. S., Dobson, C. M., & Griffin, R. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625999 · Cited by 253
Self-citationHou, G., Yan, S., Trébosc, J., Amoureux, J.-P., & Polenova, T. (2013) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2013.04.009 · Cited by 193
In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
Ghosh, R., Xiao, Y., Kragelj, J., & Frederick, K. K. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c06680 · Cited by 66
Bahri, S., Safeer, A., Adler, A., Smedes, H., van Ingen, H., & Baldus, M. (2023) · Journal of Biomolecular NMR · doi:10.1007/s10858-023-00415-6 · Cited by 31
Costello, W. N., Xiao, Y., Mentink-Vigier, F., Kragelj, J., & Frederick, K. K. (2024) · Journal of Biomolecular NMR · doi:10.1007/s10858-024-00436-9 · Cited by 16
Metadata
- Authors
- Jaroniec, C. P., Filip, C., & Griffin, R. G.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-08-15
- Volume
- 124
- Issue
- 36
- Pages
- 10728-10742
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2100055535
- Cited by
- 288
- References
- 29
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
