Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.

TL;DR: It is proposed that amyloids could have existed in a prebiotic world, and may have been the first functional protein fold in living cells, and further speculate about currently undocumented biological roles for the amyloid entity.

TL;DR: The results underscore the utility of the limited proteolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics-function relationships of a novel and rare protein, especially if available in minute amounts.

TL;DR: Recent experimental and theoretical advances in the elucidation of the conformational properties of dynamic, heterogeneous and/or insoluble protein ensembles populated on complex, multidimensional protein energy landscapes are described.

TL;DR: This approach assessed the structural features of more than 1,000 yeast proteins simultaneously and detected altered conformations for ∼300 proteins upon a change of nutrients, finding that some branches of carbon metabolism are transcriptionally regulated whereas others are regulated by enzyme conformational changes.

TL;DR: Thioflavine T associates rapidly with aggregated fibrils of the synthetic β/A4‐derived peptides β( 1–28) and β(1–40), giving rise to a new excitation maximum at 450 nm and enhanced emission at 482 nm, as opposed to the 385 nm and 445 nm of the free dye.

TL;DR: This paper is a contribution from the Oxford Centre for Molecular Sciences, which is funded by the BBSRC, EPSRC and MRC.

TL;DR: A simple mechanistic model has emerged for both processes that involves a nucleation-dependent polymerization that dictates that aggregation is dependent on protein concentration and time.

TL;DR: The histologic benzothiazole dyes thioflavin S and thioFLavin T under the appropriate conditions selectively stain amyloid structures in a number of pathological settings, as does the diazobenzidine sulfonate dye, Congo red, which is also birefringent when bound to fibrils.