There are multiple definitions for low complexity regions (LCRs) in protein sequences, with
all of them broadly considering LCRs as regions with fewer amino acid types compared to …

Intrinsically disordered/unstructured proteins exist without a stable three-dimensional (3D)
structure as highly flexible conformational ensembles. The available genome sequences …

While the majority of proteins with available structures are able to fold independently and
mediate interactions only after acquiring their folded state, a subset of the known protein …

The noncovalent forces that stabilize protein structures are not fully understood. One way to
address this is to study equilibria between unfolded states and α-helices in peptides …

The swinging crossbridge hypothesis states that energy from ATP hydrolysis is transduced
to mechanical movement of the myosin head while bound to actin. The light chain-binding …

Low complexity regions (LCRs) in protein sequences are characterized by a less diverse
amino acid composition compared to typically observed sequence diversity. Recent studies …

Ionizable residues can release and take up protons and this has an influence on protein
structure and function. The extent of protonation is linked to the overall pH of the solution …

Waggawagga is a web-based tool for the comparative visualization of coiled-coil predictions
and the detection of stable single α-helices (SAH domains). Overview schemes show the …

The chromosome passenger complex (CPC) is a master regulator of mitosis. Inner
centromere protein (INCENP) acts as a scaffold regulating CPC localization and activity …

The modification of adenosine to inosine at the wobble position (I34) of tRNA anticodons is
an abundant and essential feature of eukaryotic tRNAs. The expansion of inosine-containing …