Co-translational protein folding is an essential process by which cells ensure the safe and
efficient production and assembly of new proteins in their functional native states following …

We present an analytical treatment of a set of coupled kinetic equations that governs the self-assembly
of filamentous molecular structures. Application to the case of protein aggregation …

Self-replicating molecules are likely to have played an important role in the origin of life, and
a small number of fully synthetic self-replicators have already been described. Yet it …

The cross-β amyloid form of peptides and proteins represents an archetypal and widely
accessible structure consisting of ordered arrays of β-sheet filaments. These complex …

An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils
reveals that this structural form is likely to be the most stable one that protein molecules can …

… Thus, given the limited sample lifetimes, in combination with the maximum working
concentrations possible for ribosomes (ca. 10 μM) and their large molecular weight (2.3 MDa), low …

The aggregation of the intrinsically disordered protein α-synuclein to form fibrillar amyloid
structures is intimately associated with a variety of neurological disorders, most notably …

… For each titration series, ca. 30 FIR resonances were fitted globally to a two-state binding …
spectra across a titration of uniformly 15 N-labelled (Ca 2+ ) 4 -CaM with TFP and attempted to …

The molecular chaperone αB-crystallin is a small heat-shock protein that is upregulated in
response to a multitude of stress stimuli, and is found colocalized with Aβ amyloid fibrils in the …

… at the peptidyl transference centre (PTC), a nascent polypeptide must pass through the
ribosomal exit tunnel, a confined environment varying between 10 and 20 Å in diameter and ca. …