Long‐lived states in an intrinsically disordered protein domain. (22nd September 2013)

• Record Type: Journal Article
• Authors: Fernandes, L.; Guerniou, C.; Marín‐Montesinos, I.; Pons, M.; Kateb, F.; Vasos, P. R.
• Is Part Of: Magnetic resonance in chemistry. Volume 51:Number 11(2013:Nov.)
• Page Start: 729
• Page End: 733
• Publication Date: 2013-09-22
• Subjects: Nuclear magnetic resonance spectroscopy -- Periodicals; Chemistry, Organic -- Periodicals; Magnetic resonance -- Periodicals; 538.36
• DOI: 10.1002/mrc.4008
• Languages: English
• ISSNs: 0749-1581

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Long‐lived states (LLS) are relaxation‐favored spin population distributions of <italic>J</italic>‐coupled magnetic nuclei. LLS were measured, along with classical ¹H and ¹⁵N relaxation rate constants, in amino acids of the N‐terminal Unique domain of the c‐Src kinase, which is disordered <italic>in vitro</italic> 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 &amp; Sons, Ltd.</p> </abstract>