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

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 …

Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or
partly and play important roles in diverse biological phenomena. Their structure dynamically …

The free energy landscape theory has been very successful in rationalizing the folding
behaviour of globular proteins, as this representation provides intuitive information on the …

Ion mobility-mass spectrometry (IM-MS) is a technology of growing importance for structural
biology, providing complementary 3D structure information for biomolecules within samples …

Electrospray-ionization mass spectrometry (ESI-MS) is widely used for protein studies. It has
been shown that the extent of protein ionization under nondenaturing conditions correlates …

Phosphorylation of intrinsically disordered proteins/regions (IDPs/IDRs) has a profound
effect in biological functions such as cell signaling, protein folding or unfolding, and long …

Electrospray‐ionization mass spectrometry (ESI‐MS) is a key tool of structural biology,
complementing the information delivered by conventional biochemical and biophysical …

Nucleoporins (Nups), which are intrinsically disordered, form a selectivity filter inside the
nuclear pore complex, taking a central role in the vital nucleocytoplasmic transport …

Mass spectrometry is now an indispensable tool in the armamentarium of molecular
biophysics, where it is used for tasks ranging from protein sequencing and mapping of post …