Structural and Conformational Prerequisites of Amyloidogenesis
Document Type
Book Chapter
Publication Date
2006
Keywords
Alzheimer Disease, Immunoglobulin Light Chain, Islet Amyloid Polypeptide, Familial Amyloid Polyneuropathy, Amyloidogenic Protein
Digital Object Identifier (DOI)
https://doi.org/10.1007/0-387-25919-8_1
Abstract
Recent reports give strong support to the idea that amyloid fibril formation and the subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. In this review recent findings are surveyed to illustrate that protein fibrillogenesis requires a partially folded conformation. This amyloidogenic conformation is relatively unfolded, and shares many structural properties with the premolten globule state, a partially folded intermediate frequently observed in the early stages of protein folding and under some equilibrium conditions. The inherent flexibility of such an intermediate is essential in allowing the conformational rearrangements necessary to form the core cross-β; structure of the amyloid fibril.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Structural and Conformational Prerequisites of Amyloidogenesis, in V. N. Uversky & A. L. Fink (Eds.), Protein Misfolding, Aggregation, and Conformational Diseases, Springer, p. 1-20
Scholar Commons Citation
Uversky, Vladimir N; Fernández, Ariel; and Fink, Anthony L., "Structural and Conformational Prerequisites of Amyloidogenesis" (2006). Molecular Medicine Faculty Publications. 1035.
https://digitalcommons.usf.edu/mme_facpub/1035
