The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Frequency Selective Heteronuclear Dipolar Recoupling in Rotating Solids: Accurate13C−15N Distance Measurements in Uniformly13C,15N-labeled Peptides
Abstract
We describe a magic-angle spinning NMR experiment for selective (13)C-(15)N distance measurements in uniformly (13)C,(15)N-labeled solids, where multiple (13)C-(15)N and (13)C-(13)C interactions complicate the accurate measurement of structurally interesting, weak (13)C-(15)N dipolar couplings. The new experiment, termed FSR (frequency selective REDOR), combines the REDOR pulse sequence with a frequency selective spin-echo to recouple a single (13)C-(15)N dipolar interaction in a multiple spin system. Concurrently the remaining (13)C-(15)N dipolar couplings and all (13)C-(13)C scalar couplings to the selected (13)C are suppressed. The (13)C-(15)N coupling of interest is extracted by a least-squares fit of the experimentally observed modulation of the (13)C spin-echo intensity to the analytical expression describing the dipolar dephasing in an isolated heteronuclear spin pair under conventional REDOR. The experiment is demonstrated in three uniformly (13)C,(15)N-labeled model systems: asparagine, N-acetyl-L-Val-L-Leu and N-formyl-L-Met-L-Leu-L-Phe; in N-formyl-[U-(13)C,(15)N]L-Met-L-Leu-L-Phe we have determined a total of 16 internuclear distances in the 2.5-6 A range.
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
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics News · doi:10.1051/epn/19861701011 · Cited by 7,989
Hahn, E. L. (1950) · Physical Review · doi:10.1103/physrev.80.580 · Cited by 5,085
Proton-enhanced NMR of dilute spins in solids
Pines, A., Gibby, M. G., & Waugh, J. S. (1973) · The Journal of Chemical Physics · doi:10.1063/1.1680061 · Cited by 2,493
Principles of High Resolution NMR in Solids
Mehring, M. (1983) · Springer eBooks · doi:10.1007/978-3-642-68756-3 · Cited by 1,981
Principles of Nucleic Acid Structure
Parish, J. (1985) · Biochemical Education · doi:10.1016/0307-4412(85)90046-9 · Cited by 1,486
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
Nuclear Magnetic Resonance Spectra from a Crystal rotated at High Speed
ANDREW, E. R., BRADBURY, A., & EADES, R. G. (1958) · Nature · doi:10.1038/1821659a0 · Cited by 1,255
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
Free Induction Decays of Rotating Solids
Lowe, I. J. (1959) · Physical Review Letters · doi:10.1103/physrevlett.2.285 · Cited by 1,170
Coherent Averaging Effects in Magnetic Resonance
Haeberlen, U., & Waugh, J. S. (1968) · Physical Review · doi:10.1103/physrev.175.453 · Cited by 1,083
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
Practical Protein Crystallography
(1999) · Elsevier eBooks · doi:10.1016/b978-0-12-486052-0.x5000-3 · Cited by 488
Antzutkin, O. N., Balbach, J. J., Leapman, R. D., Rizzo, N. W., Reed, J., & Tycko, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.230315097 · Cited by 383
Dipolar recoupling in MAS spectra of biological solids
Griffin, R. (1998) · Nature Structural Biology · doi:10.1038/749 · Cited by 345
Self-citationMassachusetts Institute of Technology
(2008) · Encyclopedia of Global Warming and Climate Change · doi:10.4135/9781412963893.n406 · Cited by 340
Determination of Membrane Protein Structure by Rotational Resonance NMR: Bacteriorhodopsin
Creuzet, F., McDermott, A., Gebhard, R., van der Hoef, K., Spijker-Assink, M. B., Herzfeld, J., Lugtenburg, J., Levitt, M. H., & Griffin, R. G. (1991) · Science · doi:10.1126/science.1990439 · Cited by 245
Self-citationBaddeleyite-Type High-Pressure Phase of TiO 2
Sato, H., Endo, S., Sugiyama, M., Kikegawa, T., Shimomura, O., & Kusaba, K. (1991) · Science · doi:10.1126/science.251.4995.786 · Cited by 198
Solid-state NMR measurement of Ψ in peptides: a NCCN 2Q-heteronuclear local field experiment
Costa, P. R., Gross, J. D., Hong, M., & Griffin, R. G. (1997) · Chemical Physics Letters · doi:10.1016/s0009-2614(97)01107-x · Cited by 170
Self-citationResonance Assignments for Solid Peptides by Dipolar-Mediated 13 C/ 15 N Correlation Solid-State NMR
Hong, M., & Griffin, R. G. (1998) · Journal of the American Chemical Society · doi:10.1021/ja980775w · Cited by 128
Self-citationHigh-resolution NMR of biological solids
McDowell, L. M., & Schaefer, J. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80028-5 · Cited by 100
Verbist, J. J., Lehmann, M. S., Koetzle, T. F., & Hamilton, W. C. (1972) · Acta Crystallographica Section B · doi:10.1107/s0567740872007368 · Cited by 97
Hohwy, M., Jaroniec, C. P., Reif, B., et al. (2000) · Journal of the American Chemical Society · doi:10.1021/ja9913737 · Cited by 93
Self-citationFreeman, R. (1998) · doi:10.1093/oso/9780198504818.001.0001 · Cited by 88
Measurement of 13C−15N Distances in Uniformly 13C Labeled Biomolecules: J-Decoupled REDOR
Jaroniec, C. P., Tounge, B. A., Rienstra, C. M., et al. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9921569 · Cited by 84
Self-citationGregory, D. M., Benzinger, T. L. S., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Meredith, S. C., & Botto, R. E. (1998) · Solid State Nuclear Magnetic Resonance · doi:10.1016/s0926-2040(98)00086-1 · Cited by 75
Griffiths, J. M., Bennett, A. E., Engelhard, M., et al. (1999) · Biochemistry · doi:10.1021/bi991106d · Cited by 41
Cited by
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687
Metadata
- Authors
- Jaroniec, C. P., Tounge, B. A., Herzfeld, J., & Griffin, R. G.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-03-22
- Volume
- 123
- Issue
- 15
- Pages
- 3507-3519
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2037844642
- Cited by
- 255
- References
- 27
- FWCI
- 8.31
- 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.
