Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and
structural transitions of biological macromolecules in solution. SAXS provides low resolution …

The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

Elastin-like polypeptides (ELPs) are a class of stimuli-responsive biopolymers inspired by
the intrinsically disordered domains of tropoelastin that are composed of repeats of the …

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 …

A longstanding question in molecular biology is the extent to which the behavior of
macromolecules observed in vitro accurately reflects their behavior in vivo. A number of …

Within the canonical repertoire of the amino acid involved in protein biogenesis, proline
plays a unique role as an amino acid presenting a modified backbone rather than a side …

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 …

Small-angle scattering of X-rays (SAXS) is an established method to study the overall
structure and structural transitions of biological macromolecules in solution. For folded …

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

Understanding signaling and other complex biological processes requires elucidating the
critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent∼ …