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Long‐lived states in an intrinsically disordered protein domain
Author(s) -
Fernandes L.,
Guerniou C.,
MarínMontesinos I.,
Pons M.,
Kateb F.,
Vasos P. R.
Publication year - 2013
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.4008
Subject(s) - chemistry , relaxation (psychology) , biomolecule , population , spin–lattice relaxation , nuclear magnetic resonance spectroscopy , spectroscopy , chemical physics , nuclear magnetic resonance , crystallography , stereochemistry , biochemistry , physics , quantum mechanics , psychology , social psychology , demography , sociology , nuclear quadrupole resonance
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. Copyright © 2013 John Wiley & Sons, Ltd.