Nanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy

Nanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy.

The amyloid state of polypeptides is a stable, highly organized structural form consisting of laterally associated β-sheet protofilaments that may be adopted as an alternative to the functional, native state. Identifying the balance of forces stabilizing amyloid is fundamental to understanding the wide accessibility of this state to peptides and proteins with unrelated primary sequences, variou...

Four-Dimensional Electron Microscopy

Four-dimensional electron microscopy.

The discovery of the electron over a century ago and the realization of its dual character have given birth to one of the two most powerful imaging instruments: the electron microscope. The electron microscope's ability to resolve three-dimensional (3D) structures on the atomic scale is continuing to affect different fields, including materials science and biology. In this Review, we highlight ...

Four-dimensional ultrafast electron microscopy.

Electron microscopy is arguably the most powerful tool for spatial imaging of structures. As such, 2D and 3D microscopies provide static structures with subnanometer and increasingly with angstrom-scale spatial resolution. Here we report the development of 4D ultrafast electron microscopy, whose capability imparts another dimension to imaging in general and to dynamics in particular. We demonst...

Nanomechanics of Amyloid Materials Studied by Atomic Force Microscopy

Amyloids are usually used to refer to a wide range of fibrous nanostructures formed from natural and synthetic proteins and peptides. The self-propagating protein aggregates are rich in ┚-sheets, which stack in hundreds to thousands units perpendicular to the fibrous axis, forming fibrils 5-15 nm in width and several micrometers in length (Dobson, 1999; Jaroniec et al., 2004; Luhrs et al., 2005...