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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
Nuclear magnetic resonance spectroscopy
Nuclear spin
Relaxation (Nuclear physics)
Protein kinases
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:
It is part of: Magnetic Resonance in Chemistry, 2013, vol. 51, p. 729-733
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ISSN: 0749-1581
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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