The development of new ion-activation/dissociation methods continues to be one of the most
active areas of mass spectrometry owing to the broad applications of tandem mass …

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Photodissociation mass spectrometry combines the ability to activate and fragment ions
using photons with the sensitive detection of the resulting product ions by mass …

The analysis of peptides and proteins as well as the grander scope of proteomics (large
scale study of proteins) has been advanced by the development of a versatile array of ion …

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 …

For about three decades, the chemistry of cation radicals derived from organic molecules
had received a major impetus from mass spectrometry. This was because cation radicals …

Peptides and proteins are chiral molecules with their structure determined by the
composition and configuration of the amino acids constituting them. Natural amino acids …

Traditionally, the d-amino acid containing peptide (DAACP) candidate can be discovered by
observing the differences of biological activity and chromatographic retention time between …

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 …