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 …

The roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …

Structural analysis of flexible macromolecular systems such as intrinsically disordered or
multidomain proteins with flexible linkers is a difficult task as high-resolution techniques are …

Alzheimer disease is characterized by abnormal protein deposits in the brain, such as
extracellular amyloid plaques and intracellular neurofibrillary tangles. The tangles are made …

In idiopathic Parkinson's disease, intracytoplasmic neuronal inclusions (Lewy bodies)
containing aggregates of the protein α-synuclein (αS) are deposited in the pigmented nuclei …

The synucleins are a family of intrinsically disordered proteins involved in various human
diseases. α‐Synuclein has been extensively characterized due to its role in Parkinson's …

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

Proteins with intrinsically disordered domains are implicated in a vast range of biological
processes, especially in cell signaling and regulation. Having solved the quaternary …

Orientational restraints such as residual dipolar couplings promise to overcome many of the
problems that traditionally limited liquid-state nuclear magnetic resonance spectroscopy …

Intrinsically disordered proteins (IDPs) are predicted to represent a significant fraction of the
human genome, and the development of meaningful molecular descriptions of these …