The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic Tumbling
Abstract
Structural characterization of biomolecules in solution by nuclear magnetic resonance (NMR) spectroscopy is based primarily on the use of interproton distances derived from homonuclear cross-relaxation experiments. Information about short time-scale dynamics, on the other hand, is obtained from relaxation rates of heteronuclear spin pairs such as 15 N- 1 H. By combining the two types of data and utilizing the dependence of heteronuclear NMR relaxation rates on anisotropic diffusional rotational tumbling, it is possible to obtain structural information about long-range motional correlations between protein domains. This approach was applied to characterize the relative orientations and mobilities of the first three zinc-finger domains of the Xenopus transcription factor TFIIIA in aqueous solution. The data indicate that the motions of the individual zinc-finger domains are highly correlated on time scales shorter than 10 nanoseconds and that the average conformation of the three-finger polypeptide is elongated.
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Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
Cited by
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Self-citationGarcı́a de la Torre, J., Huertas, M. L., & Carrasco, B. (2000) · Journal of Magnetic Resonance · doi:10.1006/jmre.2000.2170 · Cited by 551
Ogata, K., Kanei-Ishii, C., Sasaki, M., Hatanaka, H., Nagadoi, A., Enari, M., Nakamura, H., Nishimura, Y., Ishii, S., & Sarai, A. (1996) · Nature Structural Biology · doi:10.1038/nsb0296-178 · Cited by 320
Model-Free Approach to the Dynamic Interpretation of Residual Dipolar Couplings in Globular Proteins
Meiler, J., Prompers, J. J., Peti, W., Griesinger, C., & Brüschweiler, R. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010002z · Cited by 284
Self-citationCampos-Olivas, R., Newman, J. L., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3475 · Cited by 119
Metadata
- Authors
- Brüschweiler, R., Liao, X., & Wright, P. E.
- Venue
- Science
- Published
- 1995-05-12
- Volume
- 268
- Issue
- 5212
- Pages
- 886-889
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085732532
- Cited by
- 322
- References
- 1
- FWCI
- 4.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Brüschweiler, R., Liao, X., & Wright, P. E. (1995). Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic Tumbling. Science. https://doi.org/10.1126/science.7754375
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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.
