Detection of methylation, acetylation and glycosylation of protein residues by monitoring 13C chemical-shift changes

Abstract

Post-translational modifications of proteins expand the diversity of the proteome by several orders of magnitude and have a profound effect on several biological processes.Their detection by experimental methods is not free of limitations such as the amount of sample needed or the use of destructive procedures to obtain the sample. Certainly, new approaches are needed and, therefore, we explore here, as a proof-of-concept, the feasibility of using 13C chemical shifts of different nuclei to detect methylation, acetylation and glycosylation of protein residues by monitoring the deviation of the 13C chemical Then, further use of this approach to select the most suitable 13 C-nucleus, with which to determine other modifications commonly seen, such as methylation of arginine and glycosylation of serine, asparagine and threonine, shows encouraging results.2

Assessing the One-Bond Cα–H Spin–Spin Coupling Constants in Proteins: Pros and Cons of Different Approaches

“…Especially when the motivation is to build lookup tables for fast numerical approximations of 1 J CαH SSCC values, as was done for chemical shifts on proteins and glycans. 24,25 Doing something similar with 1 J CαH SSCC will require a more complex model including non-covalent effects of the environment. This approach would be computationally very costly but most importantly, difficult to generalize to the construction of lookup tables for fast computation.…”