Recognition of the natural abundance and functional importance of intrinsically disordered
proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions …

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 …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

NMR spectroscopy is a powerful tool for biologists interested in the structure, dynamics, and
interactions of biological macromolecules. This review aims at presenting in an accessible …

Abstract Motivation: Intrinsically disordered proteins (IDPs) represent a significant fraction of
the human proteome. The classical structure function paradigm that has successfully …

“What's in a name? That which we call a rose By any other name would smell as sweet.”
From “Romeo and Juliet”, William Shakespeare (1594) This article opens a series of …

Single-molecule spectroscopy has developed into an important method for probing protein
structure and dynamics, especially in structurally heterogeneous systems. A broad range of …

Biomolecules adopt a dynamic ensemble of conformations, each with the potential to
interact with binding partners or perform the chemical reactions required for a multitude of …

Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to
structural biology due to the inapplicability of standard methods for characterization of folded …

Intrinsically disordered proteins (IDPs), which in isolation do not adopt a well-defined tertiary
structure but instead populate a structurally heterogeneous ensemble of interconverting …