Affordable Access

deepdyve-link
Publisher Website

Long-lived states in an intrinsically disordered protein domain.

Authors
  • Fernandes, L
  • Guerniou, C
  • Marín-Montesinos, I
  • Pons, M
  • Kateb, F
  • Vasos, P R
Type
Published Article
Journal
Organic Magnetic Resonance
Publisher
Wiley (John Wiley & Sons)
Publication Date
Nov 01, 2013
Volume
51
Issue
11
Pages
729–733
Identifiers
DOI: 10.1002/mrc.4008
PMID: 25941036
Source
Medline
Keywords
License
Unknown

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.

Report this publication

Statistics

Seen <100 times