Abstract
Protein aggregation via nonnative conformational states is effectively irreversible for a variety of systems of scientific and commercial interest, particularly during processing and storage. The formation of irreversible aggregates typically involves one or more reversible conformational changes leading to nonnative, aggregation-prone conformers that subsequently assemble to form soluble or insoluble aggregates. Experimentally observed kinetics of this process are controlled by a combination of the dynamics and thermodynamics of conformational transitions and association or assembly steps.
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Roberts, C.J. (2006). Nonnative Protein Aggregation. In: Misbehaving Proteins. Springer, New York, NY. https://doi.org/10.1007/978-0-387-36063-8_2
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DOI: https://doi.org/10.1007/978-0-387-36063-8_2
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