Mass spectrometry (MS) has become one of the key technologies of structural biology. In this
review, the contributions of chemical cross-linking combined with mass spectrometry (XL …

Ribonucleoprotein (RNP) granules are membrane-less organelles consisting of RNA-
binding proteins (RBPs) and RNA. RNA granules form through liquid–liquid phase …

In the 1960s, Christian Anfinsen postulated that the unique three-dimensional structure of a
protein is determined by its amino acid sequence. This work laid the foundation for the …

Post-translational modifications (PTMs) produce significant changes in the structural
properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes …

Unlike the complex glycans decorating the cell surface, the O-linked β-N-acetyl glucosamine
(O-GlcNAc) modification is a simple intracellular Ser/Thr-linked monosaccharide that is …

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

The intracellular environment represents an extremely crowded milieu, with a limited amount
of free water and an almost complete lack of unoccupied space. Obviously, slightly salted …

Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …

Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent
bonds on the backbones or amino acid side chains of proteins and expand the diversity of …

Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)
are functional proteins and domains that devoid stable secondary and/or tertiary structure …