Three-Dimensional Structural Analysis of Amyloid Fibrils by Electron Microscopy.

Amyloid fibrils are insoluble aggregates that result from the self-assembly of partially unfolded proteins. Regardless of the native structure of the precursor proteins, the predominant secondary structure in the fibrillar form is β-sheet. Proteins that form amyloid in vivo are associated with numerous diseases, including Alzheimer's, Parkinson's, and prion diseases. The three-dimensional structures of amyloid fibrils may provide valuable information on the misfolded protein conformations and on the pathways that lead to disease. The purpose of this chapter is to introduce electron microscopy as a tool for the structure determination of amyloid fibrils. [ABSTRACT FROM AUTHOR]