Mass spectrometry-based biomolecular analyses have become permanent fixtures of
academic, industrial, and clinical research settings. The rise in utilization of mass …

Peptidomics is an emerging field branching from proteomics that targets endogenously
produced protein fragments. Endogenous peptides are often functional within the body …

In nature, amino acids are found in two forms, L and D enantiomers, except for glycine which
does not have a chiral center. The change of one form to the other will lead to a change in …

Mass spectrometry (MS) is widely used in proteomic analysis but cannot differentiate
between molecules with the same mass-to-charge ratio. Nanopore technology might provide …

Proteins are composed exclusively of l-amino acids. Among elderly individuals, however, d-
aspartic acid (d-Asp) residues have been found in eye lens and brain, as well as in other …

Single cell analysis strives to probe molecular heterogeneity in morphologically similar cell
populations through quantitative or qualitative measurements of genetic, proteomic, or …

Ion mobility spectrometry (IMS) coupled to mass spectrometry (MS) has seen spectacular
growth over the last two decades. Increasing IMS sensitivity and capacity with improvements …

Proteinaceous aggregation is a well-known observable in Alzheimer's disease (AD), but
failure and storage of lysosomal bodies within neurons is equally ubiquitous and actually …

Despite often minute concentrations in vivo, d-amino acid containing peptides (DAACPs) are
crucial to many life processes. Standard proteomics protocols fail to detect them as d/l …

A receptor binding class of d-amino acid-containing peptides (DAACPs) is formed in animals
from an enzymatically mediated post-translational modification of ribosomally translated all-l …