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 …

Mass spectrometry is a vital tool for molecular characterization, and the allied technique of
ion mobility is enhancing many areas of (bio) chemical analysis. Strong synergy arises …

The combination of mass spectrometry and ion mobility spectrometry (IMS) employing a
temperature-variable drift cell or a drift tube divided into sections to make IMS-IMS …

Stabilities and structure (s) of proteins are directly coupled to their local environment or
Gibbs free energy landscape as defined by solvent, temperature, pressure, and …

The three‐dimensional structures adopted by proteins are predicated by their many
biological functions. Mass spectrometry has played a rapidly expanding role in protein …

Ion mobility and mass spectrometry techniques are coupled with a temperature-controlled
electrospray ionization source to follow the structural transitions of ubiquitin in aqueous …

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 …

The isotopic exchange approach is in use since the first observation of such reactions in
1933 by Lewis. This approach allows the investigation of the pathways of chemical and …

Key to native ion mobility/mass spectrometry is to prevent the structural denaturation of
biological molecules in the gas phase. Here, we systematically assess structural changes …

Ultraviolet photodissociation (UVPD) of gas-phase proteins has attracted increased attention
in recent years. This growing interest is largely based on the fact that, in contrast to slow …