Work

Protein aggregation processes: In search of the mechanism

Year: 2007

Type: review

Abstract: Amyloid formation typically follows a time course in which there is a long lag period followed by a rapid formation of fibrils. In this review, I show that the standard mechanisms of polymerization need to be expanded to consider that the monomeric proteins/peptides involved in amyloid formation are intrinsically disordered and exist as an ensemble of disordered-collapsed states. The review focuses primarily on events which occur in the long lag period defining these as protein folding issues, coupled with formation of oligomers. Experimental methods to explore folding and oligomerization issues over a wide range of protein concentrations using primarily fluorescence and 19F-NMR methods are discussed.

Source: Protein Science

DOI: 10.1110/ps.073164107

Author: Carl Frieden

Institution: Washington University in St. Louis

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: G1249689085, Intermediates in Protein Folding