Comparison of Partially Denatured Cytochrome Structural Ensembles in Solution and Gas Phases Using Cross-Linking Mass Spectrometry.

Electrospray ionization mass spectrometry (ESI-MS) can retain intact protein structures, but details about partially folded and unfolded protein structures during and after introduction to the gas phase are elusive. Here we use ESI-MS with chemical cross-linkers to compare denatured cytochrome structures in both solution and gas phases. Solution phase cross-linking prior to ESI captures solution phase structures, while gas phase cross-linking through ion/ion reactions in the trap cell captures gas phase structures.

Impact of lesion morphology on stent elongation during bifurcation PCI: an in vivo OCT study.

Background: Recent observations in silico and in vivo reported that, during proximal optimisation technique, drug-eluting stents (DES) elongate, challenging conventional wisdom. The interaction between plaque morphology and radial expansion is well established, but little is known about the impact of plaque morphology on elongation.

Aims: We aimed to assess the longitudinal mechanical behaviour of contemporary DES in vivo and evaluate the relationship between post-percutaneous coronary intervention (PCI) stent elongation and lesion morphology, as assessed with optical coherence tomography (OCT).

Revealing the Fates of Proteins in the Gas Phase.

The ability to observe intact proteins by native mass spectrometry allows measurements of size, oligomeric state, numbers and types of ligands and post translational modifications bound, among many other characteristics. These studies have the potential to, and in some cases are, advancing our understanding of the role of structure in protein biology and biochemistry. However, there are some long-unresolved questions about to what extent solution-like structures persist without solvent in the vacuum of the mass spectrometer.