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 …

One of the core standards of biochemistry is that the function of a protein relies on its 3D
structure. This idea posits that all the information required for a protein to perform its …

How genetic information gained its exquisite control over chemical processes needed to
build living cells remains an enigma. Today, the aminoacyl-tRNA synthetases (AARS) …

Although chaperone‐assisted protein crystallization remains a comparatively rare
undertaking, the number of crystal structures of polypeptides fused to maltose‐binding …

Abstract Measles, Nipah and Hendra viruses are severe human pathogens within the
Paramyxoviridae family. Their non-segmented, single-stranded, negative-sense RNA …

The phosphoprotein gene of the paramyxoviruses encodes multiple protein products. The P,
V, and W proteins are generated by transcriptional slippage. This process results in the …

Measles virus (MeV) and all Paramyxoviridae members rely on a complex polymerase
machinery to ensure viral transcription and replication. Their polymerase associates the …

In this review, we summarize computational and experimental data gathered so far showing
that structural disorder is abundant within paramyxoviral nucleoproteins (N) and …

The content of intrinsically disordered protein (IDP) is related to organism complexity,
evolution, and regulation. In the Plantae, despite their high complexity, experimental …

Intrinsically disordered proteins (IDPs) form biologically active complexes that can retain a
high degree of conformational disorder, escaping structural characterization by conventional …