Increasing the temperature by just a few degrees may lead to structural perturbation or
unfolding of the protein and consequent loss of function. The concepts of flexibility and …

Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of
intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This …

The paradigmatic disordered protein tau plays an important role in neuronal function and
neurodegenerative diseases. To disentangle the factors controlling the balance between …

The most commonly occurring intrinsically disordered proteins (IDPs) are polyampholytes,
which are defined by the duality of low net charge per residue and high fractions of charged …

Many proteins require different structural states or conformations for function, and
intrinsically disordered proteins, ie proteins without stable three-dimensional structure, are …

Recent advances in the structural biology of disease-relevant α-synuclein fibrils have
revealed a variety of structures, yet little is known about the process of fibril aggregate …

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a
stable three-dimensional structure, but rather adopt many different conformations in dynamic …

Single-molecule Förster resonance energy transfer (FRET) is a versatile technique for
probing the structure and dynamics of biomolecules even in heterogeneous ensembles …

Intrinsically disordered proteins (IDPs) constitute a large fraction of the human proteome and
are critical in the regulation of cellular processes. A detailed understanding of the …

Random heteropolymers (RHPs) are an interesting class of materials useful in many
theories and applications. While previous studies typically focused on simplified RHP …