Entire functional proteins as well as large regions of proteins lack structural elements which
are resolvable via crystallography or NMR. These intrinsically disordered proteins (IDPs) or …

The link between structure and function of a given protein is a principal tenet of biology. The
established approach to understand the function of a protein is to 'solve'its structure and …

Intrinsically disordered proteins do not adopt well-defined native structures and therefore
present an intriguing challenge in terms of structural elucidation as they are relatively …

Intrinsically disordered proteins (IDPs) and regions of intrinsic disorder (IDRs) are abundant
in proteomes and are essential for many biological processes. Thus, they are often …

Inherent disorder is an integral part of all proteomes, represented as fully or partially
unfolded proteins. The lack of order in intrinsically disordered proteins (IDPs) results in an …

In the last ten years mass spectrometry has emerged as a powerful biophysical technique
capable of providing unique insights into the structure and dynamics of proteins. Part of this …

In recent years both mass spectrometry (MS) and ion mobility mass spectrometry (IM‐MS)
have been developed as techniques with which to study proteins that lack a fixed tertiary …

Intrinsically disordered proteins (IDPs) are integral part of the proteome, regulating vital
biological processes. Such proteins gained further visibility due to their key role in …

The coupling of electrospray ionization (ESI) with ion mobility-mass spectrometry (IM-MS)
allows structural studies on biological macromolecules in a solvent-free environment …

Native mass spectrometry (MS) has become a central tool of structural proteomics, but its
applicability to the peculiar class of intrinsically disordered proteins (IDPs) is still object of …