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 …

Mass spectrometry-based methods have become increasingly important in structural biology—
in particular for large and dynamic, even heterogeneous assemblies of biomolecules. Native …

Native ion mobility-mass spectrometry (IM-MS) is a rapidly growing field for studying the
composition and structure of biomolecules and biomolecular complexes using gas-phase …

In the past decade, mass spectrometry (MS) coupled with electrospray ionization (ESI) has
been extensively applied to the study of intact proteins and their complexes, often without …

The precise relationship between native gas-phase protein ion structure, charge,
desolvation, and activation remains elusive. Much evidence supports the Charge Residue …

Melittin is a 26 residue peptide and the major component of bee (Apis mellifera) venom.
Although melittin has both anticancer and antimicrobial properties, utilization has been …

Molecular dynamics (MD) simulations are used to model changes in the conformational
preferences of a model peptide during the transition from a hydrated environment (charged …

Careful transfer of ions into the gas-phase permits the measurement of protein structures,
with ion mobility-mass spectrometry, which provides shape and stoichiometry information …

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 demonstrate the capabilities of a laser-coupled ion mobility mass spectrometer for
analysis of peptide sequence and structure showing ultraviolet photodissociation (UVPD) …