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2013-09-22

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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/47994

Long-lived States in an intrinsically disordered protein domain

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http://dx.doi.org/10.1002/mrc.4008

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.

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Espectroscòpia de ressonància magnètica nuclear, Spin (Física nuclear), Relaxació (Física nuclear), Proteïnes quinases, Bioquímica

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Nuclear magnetic resonance spectroscopy, Nuclear spin, Relaxation (Nuclear physics), Protein kinases, Biochemistry

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Articles publicats en revistes (Química Inorgànica i Orgànica)

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FERNANDES, L., et al. Long-lived States in an intrinsically disordered protein domain. Magnetic Resonance in Chemistry. 2013. Vol. 51, num. 729-733. ISSN 0749-1581. [consulted: 7 of June of 2026]. Available at: https://hdl.handle.net/2445/47994

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