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 …

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 …

Matrix assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is a
powerful technology used to investigate the spatial distributions of thousands of molecules …

Protein–protein interfaces and architecture are critical to the function of multiprotein
complexes. Mass spectrometry-based techniques have emerged as powerful strategies for …

Mass spectrometry (MS) has played an increasingly important role in the identification and
structural and functional characterization of proteins. In particular, the use of tandem mass …

Characterization of all gas-phase charge sites of natively sprayed proteins and peptides is
demonstrated using 193 nm UVPD. The high sequence coverage offered by UVPD is …

We report the implementation of proton transfer reactions (PTR) and ion parking on an
Orbitrap mass spectrometer. PTR/ion parking allows charge states of proteins to be focused …

Tandem mass spectrometry (MS2) is a widely used method in structural analysis and
biopolymer sequencing.[1] In MS2, an ion of interest is isolated, activated, and brought to …

We revisited the implementation of 193 nm ultraviolet photodissociation (UVPD) within the
ion cyclotron resonance (ICR) cell of a Fourier transform–ion cyclotron resonance (FT-ICR) …