Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy

Juan Lopez, Robert Schneider, Francois Xavier Cantrelle, Isabelle Huvent, Guy Lippens

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

17 Citas (Scopus)

Resumen

Under physiological conditions, studies of intrinsically disordered proteins (IDPs) by conventional NMR methods based on proton detection are severely limited by fast amide-proton exchange with water.13C detection has been proposed as a solution to the exchange problem, but is hampered by low sensitivity. We propose a new pulse sequence combining proton–nitrogen cross-polarization and carbonyl detection to record high-resolution, high-sensitivity NMR spectra of IDPs under physiological conditions. To demonstrate the efficacy of this approach, we recorded a high-quality N–CO correlation spectrum of α-synuclein in bacterial cells at 37 °C.
Idioma originalEspañol
Páginas (desde-hasta)7418-7422
Número de páginas5
PublicaciónAngewandte Chemie - International Edition
Volumen55
EstadoPublicada - 20 jun. 2016

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