Native mass spectrometry (nMS) has emerged as an important tool in studying the structure
and function of macromolecules and their complexes in the gas phase. In this review, we …

Small molecule drug discovery has been propelled by the continual development of novel
scientific methodologies to occasion therapeutic advances. Although established …

Native mass spectrometry (nMS) is evolving into a workhorse for structural biology. The
plethora of online and offline preparation, separation, and purification methods as well as …

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 …

Progress in structural biology research has led to a high demand for powerful and yet
complementary analytical tools for structural characterization of proteins and protein …

Chaperonins are nanomachines that harness ATP hydrolysis to power and catalyze protein
folding, a chemical action that is directly linked to the maintenance of cell function through …

Native ion mobility mass spectrometry (nIM-MS) has emerged as a useful technology for the
rapid evaluation of biomolecular structures. When combined with collisional activation in a …

The recent discovery of asymmetric arrangements of trimers in the tautomerase superfamily
(TSF) adds structural diversity to this already mechanistically diverse superfamily …

Variable-temperature electrospray ionization (vT-ESI) native mass spectrometry (nMS) is
used to determine the thermodynamics for stepwise binding of up to 14 ATP molecules to …

Post-translational modifications (PTMs) are ubiquitous and key to regulating protein function.
Understanding the dynamics of individual PTMs and their biological roles requires robust …