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 …

A variety of membraneless organelles, often termed “biological condensates”, play an
important role in the regulation of cellular processes such as gene transcription, translation …

Proteins may vary from being rigid to having flexible regions to being completely disordered,
either as an intrinsically disordered protein (IDP) or having specific intrinsically disordered …

Intrinsically disordered proteins (IDPs) are abundant in eukaryotic proteomes, play a major
role in cell signaling, and are associated with human diseases. To understand IDP function it …

A novel esterase (est3S) gene, 1026 bp in size, was cloned from a metagenomic library
made of uncultured microorganisms from the contents of cow rumen. The esterolytic enzyme …

Large-scale cancer genome sequencing has enabled the catalogs of somatic mutations;
however, the mutational impact on intrinsically disordered protein regions (IDRs) has not …

Introduction Mutations in the RPGR gene are responsible for one of the most prevalent and
severe types of retinitis pigmentosa. Gene therapy has shown great promise to treat …

Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure. Hence, they
are often misconceived to present a challenge to Anfinsen's dogma. However, IDPs exist as …

Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs)
note the high entropy at individual sequence positions and in conformations sampled in …