title: Impact of selective excitation on carbon longitudinal relaxation: Towards fast solid-state NMR techniques.
abstract: The effect of selective pulses on the apparent carbon longitudinal relaxation is investigated in three fully (13)C-labeled systems, histidine as a model system and two proteins MerP and YajG. It is shown that the longitudinal relaxation of a selectively excited carbon spin is greatly enhanced, mainly because of fast spin-diffusion. This relaxation enhancement allows reducing the time necessary for polarization recovery between two experiments. This effect can be exploited either to improve the sensitivity of NMR experiments or to reduce the experimental time. Using selective carbon excitation combined with fast pulsing on fully (13)C-labeled proteins, a sensitivity improvement of 20-45% over standard cross-polarization methods is predicted from the measured relaxation times.
authors: Laboratoire de Chimie Inorganique et Biologique (UMR-E3 CEA/UJF, FRE 3200 CEA/CNRS), INAC, CEA, F-38054 Grenoble, France.
authors: Mathilde
authors: M
authors: Giffard
authors: Michel
authors: M
authors: Bardet
authors: Beate
authors: B
authors: Bersch
authors: Jacques
authors: J
authors: Covès
authors: Sabine
authors: S
authors: Hediger
mesh_terms: D000465:Algorithms; D002244:Carbon / Q000737:chemistry*; D049921:Cupriavidus / Q000737:chemistry; D004269:DNA, Bacterial / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D006639:Histidine / Q000737:chemistry; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011506:Proteins / Q000737:chemistry
chemical_list: D004269:DNA, Bacterial; C086060:MerP protein, Bacteria; D011506:Proteins; D006639:Histidine; D002244:Carbon