Long-lived states in an intrinsically disordered protein domain

authors	L. Fernandes, C. Guerniou, I. Marín-Montesinos, M. Pons, F. Kateb and P.R. Vasos
nationality	International
journal	Magnetic Resonance in Chemistry
abstract	Long-lived states (LLS) are relaxation-favored spin population distributions of J-coupled magnetic nuclei. LLS were measured, along with classical (1)H and (15)N relaxation rate constants, in amino acids of the N-terminal Unique domain of the c-Src kinase, which is disordered in vitro under physiological conditions. The relaxation rates of LLS can probe motions and interactions in biomolecules. LLS of the aliphatic protons of glycines, with lifetimes approximately four times longer than their spin-lattice relaxation times, are reported for the first time in an intrinsically disordered protein domain. LLS relaxation experiments were integrated with 2D spectroscopy methods, further adapting them for studies on proteins.
year published	2013
volume	51
beginning page	729
digital object identifier (doi)	10.1002/mrc.4008