Water is essential for life in many ways, and without it biomolecules might no longer truly be
biomolecules. In particular, water is important to the structure, stability, dynamics, and …

Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …

The mechanism of denaturation of proteins by urea is explored by using all-atom
microseconds molecular dynamics simulations of hen lysozyme generated on BlueGene/L …

For more than a century, urea has been commonly used as an agent for denaturing proteins.
However, the mechanism behind its denaturing power is still not well understood. Here we …

The molecular mechanism of urea-induced protein denaturation is not yet fully understood.
Mainly two opposing mechanisms are controversially discussed, according to which either …

Nonfibrillar soluble oligomers, which are intermediates in the transition from monomers to
amyloid fibrils, may be the toxic species in Alzheimer's disease. To monitor the early events …

Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …

Quantitative understanding of the kinetics of fibril formation and the molecular mechanism of
transition from monomers to fibrils is needed to obtain insights into the growth of amyloid …

Though urea is commonly used to denature proteins, the molecular mechanism of its
denaturing ability is still a subject of considerable debate. Previous molecular dynamics …

Intrinsically disordered proteins (IDPs) are a unique class of proteins that have no stable
native structure, a feature that allows them to adopt a wide variety of extended and compact …