Amyloid diseases, including neurodegenerative diseases such as Alzheimer's and
Parkinson's, are linked to a poorly understood progression of protein misfolding and …

Soft materials in nature are formed through reversible supramolecular assembly of
biological polymers into dynamic hierarchical networks. Rational design has led to self …

The tendency for proteins to form aggregates is an inherent part of every proteome and
arises from the self-assembly of short protein segments called aggregation-prone regions …

Many chaperones favour binding to hydrophobic sequences that are flanked by basic
residues while disfavouring acidic residues. However, the origin of this bias in protein quality …

Tryptophan as an aromatic amino acid with a hydrophobic indole group plays important
roles in stabilizing protein structures and enhancing molecular bindings in nature, but was …

Non-covalent interactions between naturally occurring aromatic residues have been widely
exploited as scaffold stabilizing agents in de novo designed peptides and in Nature …

We present an analysis of the most extensive explicit-solvent simulations of β-hairpins to
date (9.4 ms in aggregate), with the aim of probing the effects of tryptophan mutations on …

Over the years, a large number of multidisciplinary investigations has unveiled that the self‐
assembly of short peptides and even of individual amino acids can generate a variety of …

Every residue on a protein can be characterized by its interaction with water, in lack or in
excess, as water is the matrix of biological systems. Infrared spectroscopy and the …

The occurrence, chemistry, resolution, and analysis of amino acids published in the
literature from 2013 finished with the year of 2016 are reviewed in this Chapter which is …