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 …

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 …

Highlights•High entropy of intrinsically disordered regions (IDRs) forms the basis for
functional plasticity.•Inherent features of IDRs are optimised to overcome the entropic cost of …

Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in
their functional states. Although this conformational plasticity is essential to their function …

Structural analysis of proteins and nucleic acids is complicated by their inherent flexibility,
conferred, for example, by linkers between their contiguous domains. Therefore, the …

Multidomain proteins containing intrinsically disordered linkers exhibit large-scale dynamic
modes that play key roles in a multitude of molecular recognition and signaling processes …

Conformational changes in nucleic acids play a key role in the way genetic information is
stored, transferred, and processed in living cells. Here, we describe new approaches that …

The characterization of denatured states of proteins is challenging because the lack of
permanent structure in these states makes it difficult to apply to them standard methods of …

Challenges in determining the structures of heterogeneous and dynamic protein complexes
have greatly hampered past efforts to obtain a mechanistic understanding of many important …

Several enzymes can simultaneously interact with multiple intracellular metabolites,
however, how the allosteric effects of distinct ligands are integrated to coordinately control …