Abstract
Visualizing a protein's molecular motions has been a long standing topic of research in the biophysics community. Largely this has been done by exploiting nuclear magnetic resonance spectroscopy (NMR), and arguably no protein's molecular motions have been better characterized by NMR than that of ubiquitin (Ub), a 76 amino acid polypeptide essential in ubiquitination - a key regulatory system within cells. Herein, we discuss ubiquitin's conformational plasticity as visualized, at atomic resolution, by more than 35 years of NMR work. In our discussions we point out the differences between data acquired in vitro, ex vivo, as well as in vivo and stress the need to investigate Ub's conformational plasticity in more biologically representative backgrounds.
| Original language | English |
|---|---|
| Article number | e202400508 |
| Journal | ChemBioChem |
| Volume | 25 |
| Issue number | 24 |
| Early online date | 14 Aug 2024 |
| DOIs | |
| Publication status | Published - Dec 2024 |
Bibliographical note
Publisher Copyright:© 2024 The Author(s). ChemBioChem published by Wiley-VCH GmbH.
Funding
The authors would like to thank M.P.C. Mulder, A.O.C. Vertegaal, and A.J.J.M Bonvin for helpful conversations. The writing of this review and studies performed by our group cited here were supported by funds from the Dutch Research Council (NWO), the European Union, and the German Research Foundation (DFG). The cover and table of contents entries utilized the following PDB IDs: 1D3Z, 1V80, 1V81, 2K39, 2MBO, and 6OQ2. Lastly, given the wealth of literature we apologize to those whose important contributions have not been cited.
| Funders | Funder number |
|---|---|
| Nederlandse Organisatie voor Wetenschappelijk Onderzoek | |
| European Commission | |
| Deutsche Forschungsgemeinschaft | 6OQ2, 2K39, 1V81, 1V80 |
Keywords
- Conformational heterogeneity
- NMR
- Post-translational modifications
- Protein dynamics
- in-cell NMR