The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …

Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a
high level of structural heterogeneity and are best described by ensembles consisting of …

Abstract Structure determination of amorphous materials remains challenging, owing to the
disorder inherent to these materials. Nuclear magnetic resonance (NMR) powder …

Structural disorder is widespread in eukaryotic proteins and is vital for their function in
diverse biological processes. It is therefore highly desirable to be able to predict the degree …

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational
plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to …

Chemical shifts contain important site-specific information on the structure and dynamics of
proteins. Deviations from statistical average values, known as random coil chemical shifts …

Recent advances in NMR methodology and techniques allow the structural investigation of
biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well …

Despite playing important roles throughout biology, molecular recognition mechanisms in
intrinsically disordered proteins remain poorly understood. We present a combination of …

The sequence–structure–function paradigm of proteins has been revolutionized by the
discovery of intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs) …

Fuzzy interactions are specific, variable contacts between proteins and other biomolecules
(proteins, DNA, RNA, small molecules) formed in accord to the cellular context. Fuzzy …