Long-lived states in an intrinsically disordered protein domain.
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.
Equipe de RMN, Laboratoire de Chimie et Biochimie Toxicologiques et Pharmacologiques, UMR8601, Université Paris Descartes - CNRS, PRES Paris Sorbonne Cité, 45, rue des Saints-Pères, 75006, Paris, France.
L
L
Fernandes
C
C
Guerniou
I
I
Marín-Montesinos
M
M
Pons
F
F
Kateb
P R
PR
Vasos
D000081247:CSK Tyrosine-Protein Kinase; D005998:Glycine / Q000737:chemistry*; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011522:Protons; D013997:Time Factors; D019061:src-Family Kinases / Q000737:chemistry*
D064267:Intrinsically Disordered Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D000081247:CSK Tyrosine-Protein Kinase; D019061:src-Family Kinases; C000631346:CSK protein, human; D005998:Glycine
15N spin; 1H spin; NMR spectroscopy; intrinsically disordered proteins; kinases; long‐lived states; relaxation