Selective detection of protein acetylation by NMR spectroscopy.

Selective detection of biomolecules and their modifications in cells is essential for understanding cell functions and diseases. We have developed an NMR pulse sequence, Ac-FIND (Acetylation-FIltered aNd eDited), which uses isotope editing/filtering techniques for selective detection of protein acetylation. Acetylation of the N-terminus and lysine side chains by N-succinimidyl acetate was selectively observed for intrinsically disordered α-synuclein and well-ordered ubiquitin.

Longitudinal Spin Order Labeling on Multiple Quantum Coherences Enables NMR Analysis of Intrinsically Disordered Proteins at Ultrahigh Resolution.

Intrinsically disordered proteins (IDPs) play an important role in cell signaling, and NMR is well-suited to study conformational ensembles and dynamics of IDPs. However, the intrinsic flexibility of IDPs often results in severe spectral overlap, which hampers accurate NMR data analysis. By labeling the longitudinal spin order of an α proton (i.

Preventive effect of protein-energy supplementation on the functional decline of frail older adults with low socioeconomic status: a community-based randomized controlled study.

Background: Chronic undernutrition is a common condition in older people with low socioeconomic status and is clearly an important component of frailty. However, it is uncertain whether protein-energy supplementation can prevent functional decline in this group.

Methods: Eighty-seven frail older adults (usual gait speed, <0.