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- W2073315105 abstract "Protein aggregation, the process by which native proteins convert into insoluble fibrillar structures, has implication in human health, biotechnology and material science. Most studies on aggregation kinetics of proteins associated with diseases indicated accumulation of critical nucleus during the process. However, little is known about the conformation of aggregation nucleus and its precursor monomer. In spite of their importance these states are difficult to characterize mainly because they form transiently in the process. In this study, we have designed the conditions and method to stabilize the monomeric aggregation precursor state of lysozyme. We report that conformation of monomeric aggregation precursor state of lysozyme regulate the accumulation and conformation of critical nucleus of the aggregation. We would also show that the polymorphism in fibrils/protofibrils thus formed is ultimately controlled by monomeric aggregation precursor state. Small molecule inhibitor and accelerator of aggregation act by binding to native state of the protein and modifying the unfolding pathway of native state and conformation of aggregation precursor state. Our study offers opportunities to investigate the small differences existing in the mechanism of formation of different kind of aggregates." @default.
- W2073315105 created "2016-06-24" @default.
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- W2073315105 date "2013-01-01" @default.
- W2073315105 modified "2023-09-29" @default.
- W2073315105 title "The Conformation of Monomeric Aggregation Precursor States Control the Aggregation of Lysozyme" @default.
- W2073315105 doi "https://doi.org/10.1016/j.bpj.2012.11.297" @default.
- W2073315105 hasPublicationYear "2013" @default.
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