Long-lived States in an intrinsically disordered protein domain
Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is disordered in vitro under physiological conditio...
| Autores: | , , , , , |
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| Formato: | artículo |
| Estado: | Versión enviada para evaluación y publicación |
| Fecha de publicación: | 2013 |
| País: | España |
| Recursos: | Universidad de Barcelona |
| Repositorio: | Dipòsit Digital de la UB |
| OAI Identifier: | oai:diposit.ub.edu:2445/47994 |
| Acesso em linha: | https://hdl.handle.net/2445/47994 |
| Access Level: | acceso abierto |
| Palavra-chave: | Espectroscòpia de ressonància magnètica nuclear Spin (Física nuclear) Relaxació (Física nuclear) Proteïnes quinases Bioquímica Nuclear magnetic resonance spectroscopy Nuclear spin Relaxation (Nuclear physics) Protein kinases Biochemistry |
| Resumo: | Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is disordered in vitro under physiological conditions. The relaxation rates of LLS are a probe for motions and interactions in biomolecules. LLS of the aliphatic protons of glycines, with lifetimes ca. four times longer than their spin-lattice relaxation times, are reported for the first time in an intrinsically disordered protein domain (IDP). LLS relaxation experiments were integrated with 2D spectroscopy methods, further adapting them for studies on proteins. |
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