Please use this identifier to cite or link to this item: 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)

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