The misfolding, amyloid aggregation, and fibril formation of intrinsically disordered
proteins/peptides (or amyloid proteins) have been shown to cause a number of disorders …

Highlights•Sparsely populated protein states can play significant biological roles.•NMR
spectroscopy can structurally and dynamically characterize 'invisible'protein states.•We …

Abstract 2D NMR is extensively used in many different fields, and its potential for the study of
complex biochemical or chemical mixtures has been widely demonstrated. 2D NMR gives …

NMR spectroscopy is a versatile tool for studying time-dependent processes: chemical
reactions, phase transitions or macromolecular structure changes. However, time-resolved …

Highlights•A range of functionally and structurally unrelated proteins form amyloid.•Toxic
intermediates remain elusive, making their targeting a significant challenge.•Design and …

Transient oligomers are commonly formed in the early stages of amyloid assembly.
Determining the structure (s) of these species and defining their role (s) in assembly is key to …

The early stages of protein misfolding and aggregation involve disordered and partially
folded protein conformers that contain a high degree of dynamic disorder. These dynamic …

Folding intermediates mediate both protein folding and the misfolding and aggregation
observed in human diseases, including amyotrophic lateral sclerosis (ALS), and are prime …

The functionality of the tumor suppressor p53 is altered in more than 50% of human cancers,
and many individuals with cancer exhibit amyloid-like buildups of aggregated p53. An …

Aggregation of initially stably structured proteins is involved in more than 20 human amyloid
diseases. Despite intense research, however, how this class of proteins assembles into …