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http://hdl.handle.net/2445/47994
Title: | Long-lived States in an intrinsically disordered protein domain |
Author: | Fernandes, L. Guerniou, C. Marín Montesinos, Ildefonso Pons Vallès, Miquel Kateb, F. Vasos, P. R. |
Keywords: | 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 |
Issue Date: | 22-Sep-2013 |
Publisher: | John Wiley & Sons |
Abstract: | 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. |
Note: | Versió preprint del document publicat a: http://dx.doi.org/10.1002/mrc.4008 |
It is part of: | Magnetic Resonance in Chemistry, 2013, vol. 51, p. 729-733 |
URI: | http://hdl.handle.net/2445/47994 |
Related resource: | http://dx.doi.org/10.1002/mrc.4008 |
ISSN: | 0749-1581 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
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