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Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium
Abstract
In isotropic solution, internuclear dipolar couplings average to zero as a result of rotational diffusion. By dissolving macromolecules in a dilute aqueous nematic discotic liquid-crystalline medium containing widely spaced magnetically oriented particles, a tunable degree of solute alignment with the magnetic field can be created while retaining the high resolution and sensitivity of the regular isotropic nuclear magnetic resonance (NMR) spectrum. Dipolar couplings between 1 H- 1 H, 1 H- 13 C, 1 H- 15 N, and 13 C- 13 C pairs in such an oriented macromolecule no longer average to zero, and are readily measured. Distances and angles derived from dipolar couplings in human ubiquitin are in excellent agreement with its crystal structure. The approach promises to improve the accuracy of structures determined by NMR, and extend the size limit.
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Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
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Metadata
- Authors
- Tjandra, N., & Bax, A.
- Venue
- Science
- Published
- 1997-11-07
- Volume
- 278
- Issue
- 5340
- Pages
- 1111-1114
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2073486807
- Cited by
- 1,719
- References
- 1
- FWCI
- 49.21
- Type
- journal article
- Language
- en
- Open access
- closed
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- Tjandra, N., & Bax, A. (1997). Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium. Science. https://doi.org/10.1126/science.278.5340.1111
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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