An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
Dissolution dynamic nuclear polarization (DNP) has become one of the predominant implementations for DNP. However, the technical implementation of transferring the sample from the polarizer to the nuclear magnetic resonance (NMR) system remains challenging. There is a need for additional technical o...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2015 |
| País: | España |
| Institución: | Universidad de Barcelona |
| Repositorio: | Dipòsit Digital de la UB |
| OAI Identifier: | oai:diposit.ub.edu:2445/138584 |
| Acceso en línea: | https://hdl.handle.net/2445/138584 |
| Access Level: | acceso abierto |
| Palabra clave: | Ubiqüitina Proteïnes Ubiquitin Proteins |
| Sumario: | Dissolution dynamic nuclear polarization (DNP) has become one of the predominant implementations for DNP. However, the technical implementation of transferring the sample from the polarizer to the nuclear magnetic resonance (NMR) system remains challenging. There is a need for additional technical optimizations in order to use dissolution DNP for biochemical and chemical applications. Here we show how a newly designed pressure dissolution kit considerably improves spectral quality and stability by enabling highly reliable and fast sample transfer to the NMR system. |
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