Membrane-less organelles assemble through liquid–liquid phase separation (LLPS) of
partially disordered proteins into highly specialized microenvironments. Currently, it is …

A central challenge in structural biology is represented by dynamic and heterogeneous
systems, as typically represented by proteins in solution, with the extreme case of …

A variety of scattering-based, microscopy-based, and mobility-based methods are frequently
used to probe the size distributions of colloidal nanoparticles with transmission electron …

Maintaining the protein high-order structures and interactions during the transition from
aqueous solution to gas phase is essential to the structural analysis of native mass …

Native ion mobility/mass spectrometry is well-poised to structurally screen proteomes but
characterizes protein structures in the absence of a solvent. This raises long-standing …

Native mass spectrometry (MS) is widely employed to study the structures and assemblies of
proteins ranging from small monomers to megadalton complexes. Molecular dynamics (MD) …

How the self-assembly of partially disordered proteins generates functional compartments in
the cytoplasm and particularly in the nucleus is poorly understood. Nucleophosmin 1 …

Current experiments only provide low-resolution information on gaseous protein ions
generated by electrospray ionization (ESI). Molecular dynamics (MD) simulations can yield …

Mass spectrometry and single molecule force microscopy are two experimental approaches
able to provide structural information on intrinsically disordered proteins (IDPs). These …

Gaussia luciferase (GLuc) is one of the most luminescent luciferases known and is widely
used as a reporter in biochemistry and cell biology. During catalysis, GLuc undergoes …