A survey of protein databases indicates that the majority of enzymes exist in oligomeric
forms, with about half of those found in the UniProt database being homodimeric …

Conspectus Protein aggregation in aqueous cellular environments is linked to diverse
human diseases. Protein aggregation proceeds through a multistep process initiated by …

Amyloid fibril deposits of the intrinsically disordered hIAPP peptide are found in 95% of type
II diabetes patients, and the aggregation of this peptide is suggested to induce apoptotic cell …

Peptide self-assembly is the process by which peptide molecules aggregate into low
dimensional (1D, 2D) or 3D ordered materials with potential applications ranging from drug …

The physics and chemistry of a charged interface are governed by the structure of the
electrical double layer (EDL). Determination of the interfacial water thickness (d iw) of the …

Understanding the molecular determinants of the relative propensities of proteins to
aggregate in a cellular environment is a central issue for treating protein‐aggregation …

Folding funnel is the essential concept of the free energy landscape for ordered proteins.
How does this concept apply to intrinsically disordered proteins (IDPs)? Here, we address …

Protein aggregation plays a critical role in the pathogenesis of neurodegenerative diseases,
and the mechanism of its progression is poorly understood. Here, we examine the structural …

Thermal-induced conformational changes and protein–protein interactions of bovine serum
albumin (BSA) in aqueous solution are assessed by small angle X-ray scattering (SAXS) at …

It is a central issue to elucidate the new type of molecular recognition accompanied by a
global structural change of a molecule upon binding to its targets. Here we investigate the …