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http://hdl.handle.net/2445/138584
Title: | An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination |
Author: | Puig-Sàrries, Pilar Bijlmakers, Marie-Jose Zuin, Alice Bichmann, Anne Pons Vallès, Miquel Crosas i Navarro, Bernat |
Keywords: | Ubiqüitina Proteïnes Ubiquitin Proteins |
Issue Date: | 10-Jun-2015 |
Publisher: | Biochemical Society |
Abstract: | 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. |
Note: | Versió postprint del document publicat a: https://doi.org/10.1042/BJ20141571 |
It is part of: | Biochemical Journal, 2015, vol. 469, num. 3, p. 455-467 |
URI: | http://hdl.handle.net/2445/138584 |
Related resource: | https://doi.org/10.1042/BJ20141571 |
ISSN: | 0264-6021 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
Files in This Item:
File | Description | Size | Format | |
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655716.pdf | 1.48 MB | Adobe PDF | View/Open |
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