The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Model-Free Approach to the Dynamic Interpretation of Residual Dipolar Couplings in Globular Proteins
Abstract
The effects of internal motions on residual dipolar NMR couplings of proteins partially aligned in a liquid-crystalline environment are analyzed using a 10 ns molecular dynamics (MD) computer simulation of ubiquitin. For a set of alignment tensors with different orientations and rhombicities, MD-averaged dipolar couplings are determined and subsequently interpreted for different scenarios in terms of effective alignment tensors, average orientations of dipolar vectors, and intramolecular reorientational vector distributions. Analytical relationships are derived that reflect similarities and differences between motional scaling of dipolar couplings and scaling of dipolar relaxation data (NMR order parameters). Application of the self-consistent procedure presented here to dipolar coupling measurements of biomolecules aligned in different liquid-crystalline media should allow one to extract in a "model-free" way average orientations of dipolar vectors and specific aspects of their motions.
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Cited by
An introduction to NMR-based approaches for measuring protein dynamics
Kleckner, I. R., & Foster, M. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.10.012 · Cited by 561
Relation between native ensembles and experimental structures of proteins
Best, R. B., Lindorff-Larsen, K., DePristo, M. A., & Vendruscolo, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511156103 · Cited by 152
Metadata
- Authors
- Meiler, J., Prompers, J. J., Peti, W., Griesinger, C., & Brüschweiler, R.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-05-26
- Volume
- 123
- Issue
- 25
- Pages
- 6098-6107
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2144731691
- Cited by
- 284
- References
- 24
- FWCI
- 11.38
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
