N,N-Diethylmethylamine as lineshape standard for NMR above 130 K.: This study explores the use of N,N-Diethylmethylamine as a lineshape standard for nuclear magnetic resonance (NMR) spectroscopy at temperatures above 130 K, providing insights into its applications in high-precision NMR analysis (Fritzsching et al., 2018).
PEGylation of peptides and proteins presents significant challenges for structural characterization due to the heterogeneity of the poly(ethylene glycol) (PEG), the number of PEG moieties attached, and the site(s) of PEGylation. In this work, a novel and powerful methodology using
The room-temperature molten salt mixture of N,N-diethyl-N-(2-methoxyethyl)-N-methylammonium bis(trifluoromethanesulfonyl) imide ([DEME][TFSI]) and lithium bis(trifluoromethanesulfonyl)imide (LiTFSI) salt is herein reported as electrolyte for application in Li-O
The steady-state reaction of trimethylamine dehydrogenase (TMADH) with the artificial electron acceptor ferricenium hexafluorophosphate (Fc(+)) has been studied by stopped-flow spectroscopy, with particular reference to the mechanism of inhibition by trimethylamine (TMA). Previous studies have suggested that the presence of
The Journal of biological chemistry, 271(23), 13401-13406 (1996-06-07)
The role played by the 6-S-cysteinyl-FMN bond of trimethylamine dehydrogenase in the reductive half-reaction of the enzyme has been studied by following the reaction of the slow substrate diethylmethylamine with a C30A mutant of the enzyme lacking the covalent flavin
The Journal of biological chemistry, 269(49), 30869-30879 (1994-12-09)
The reductive half-reaction of trimethylamine dehydrogenase has been studied using the substrate diethylmethylamine over the pH range 6-10. It is found that the reaction occurs with three distinct and, under most conditions, fully resolved kinetic phases. The hyperbolic substrate concentration
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