Long-lived states in an intrinsically disordered protein domain

Long-lived states in an intrinsically disordered protein domain

Copyright © 2013 John Wiley & Sons, Ltd.

Bibliographische Detailangaben
Veröffentlicht in:Magnetic resonance in chemistry : MRC. - 1985. - 51(2013), 11 vom: 28. Nov., Seite 729-33
1. Verfasser: Fernandes, L (VerfasserIn)
Weitere Verfasser: Guerniou, C, Marín-Montesinos, I, Pons, M, Kateb, F, Vasos, P R
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Magnetic resonance in chemistry : MRC
Schlagworte:Journal Article Research Support, Non-U.S. Gov't 15N spin 1H spin NMR spectroscopy intrinsically disordered proteins kinases long‐lived states relaxation Intrinsically Disordered Proteins mehr... Nitrogen Isotopes Protons CSK Tyrosine-Protein Kinase EC 2.7.10.2 src-Family Kinases CSK protein, human EC 2.7.10.23 Glycine TE7660XO1C
Beschreibung
Zusammenfassung:Copyright © 2013 John Wiley & Sons, Ltd.
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
Beschreibung:Date Completed 08.10.2015
Date Revised 10.12.2019
published: Print-Electronic
Citation Status MEDLINE
ISSN:1097-458X
DOI:10.1002/mrc.4008