The DOI matches its Crossref record.
Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition
Open accessAbstract
Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four β-strands separated by up to 15 Å in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network.
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Citations
Cited by
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Allostery without a conformational change? Revisiting the paradigm
Nussinov, R., & Tsai, C.-J. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.11.005 · Cited by 202
Metadata
- Authors
- Fenwick, R. B., Esteban-Martín, S., Richter, B., Lee, D., Walter, K. F. A., Milovanovic, D., Becker, S., Lakomek, N. A., Griesinger, C., & Salvatella, X.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-06-20
- Volume
- 133
- Issue
- 27
- Pages
- 10336-10339
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2004577830
- Cited by
- 178
- References
- 0
- FWCI
- 8.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
