Intrinsically disordered proteins (IDPs) are proteins that perform important biological
functions without well‐defined structures under physiological conditions. IDPs can form …

Intrinsically disordered proteins (IDPs) are highly prevalent and play important roles in
biology and human diseases. It is now also recognized that many IDPs remain dynamic …

Liquid–liquid phase separation (LLPS) of some IDPs/IDRs can lead to the formation of the
membraneless organelles in vitro and in vivo, which are essential for many biological …

The cardiac sarcomere is a cellular structure in the heart that enables muscle cells to
contract. Dozens of proteins belong to the cardiac sarcomere, which work in tandem to …

Highlights•Many aspects of transcription factor function involve folding upon
binding.•Intrinsic disorder plays a role in both DNA binding and transcriptional activation.• …

Biomolecular recognition usually leads to the formation of binding complexes, often
accompanied by large-scale conformational changes. This process is fundamental to …

ABSTRACT Streptococcus pyogenes (Sp) Cas9 has been widely utilized to edit genomes
across diverse species. To achieve high efficiency and specificity as a gene editing enzyme …

Interaction between the cap-binding protein eIF4E and the scaffolding protein eIF4G is
essential for the cap-dependent translation initiation in eukaryotes. In the Saccharomyces …

Calmodulin (CaM) is a highly-expressed Ca 2+ binding protein known to bind hundreds of
protein targets. Its binding selectivity to many of these targets is partially attributed to the …

The disordered PEVK region of titin contains two main structural motifs: PPAK and poly-E.
The distribution of these motifs in the PEVK region contributes to the elastic properties of this …