Molecular Mechanisms of Protein Misfolding
Protein Misfolding, Protein Aggregation, Protein Fibrillation, Conformational Diseases, Amyloid Fibril, Oligomer, Amorphous Aggregate
Digital Object Identifier (DOI)
Unlike folded proteins that possess a single native fold that is determined only by their amino acid sequence, protein aggregates (fibrils and oligomers) are structurally highly diverse. The core of amyloid fibrils is composed of stacks of β-sheets, providing their structure with a high level of stability. High variability of packing arrangements within the fibril allows the same polypeptide chain to form amyloid fibrils with different tertiary structures. Fibrils propagate their tertiary structure by seeding; however, this process is imperfect and it results in structural alterations. Amyloid oligomers are the smaller aggregates; they have even higher conformational flexibility. Oligomers usually also rely on β-sheet stacking for intermolecular interactions, although there is a much higher degree of disorder in their structure compared to fibrils. Many oligomers are also capable of self-propagation by seeding. In this chapter we describe the mechanism of formation and the structural features of protein aggregates.
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Citation / Publisher Attribution
Molecular Mechanisms of Protein Misfolding, in V. N. Uversky & Y. L. Lyubchenko (Eds.), Bio-nanoimaging: Protein Misfolding and Aggregation, Academic Press, p. 1-14
Scholar Commons Citation
Breydo, Leonid and Uversky, Vladimir N., "Molecular Mechanisms of Protein Misfolding" (2014). Molecular Medicine Faculty Publications. 1104.