Depending on external conditions, native proteins may change their structure and undergo
different association routes leading to a large scale polymorphism of the aggregates. This …

The “dynamic” or “glass” transition in biomolecules is as important to their functioning as the
folding process. This transition occurs in the low temperature regime and has been related …

Understanding how proteins work requires a thorough understanding of their internal
dynamics. Proteins support a wide range of motions, from the femtoseconds to seconds time …

Amyloid and amyloid-like fibrils are a general class of protein aggregates and represent a
central topic in life sciences for their involvement in several neurodegenerative disorders …

The subtle interplay between long range electrostatic forces, hydrophobic interactions and
short range protein–protein interactions regulates the onset/evolution of protein aggregation …

The softness and rigidity of proteins are reflected in the structural dynamics, which are in turn
affected by the environment. The characteristic low-frequency vibrational spectrum of a …

We report on how low-frequency Raman measurements can be used as a facile tool to
investigate the supramolecular structure of amyloid fibrils. We investigate the low-frequency …

Water is abundant on earth and in the atmosphere and the most crucial liquid for life as we
know it. It has been subject to rather intense research since more than a century and still …