Analyzing The Code Of Protein Self Organization Process

3055 Words13 Pages
1 Introduction:
Protein aggregation, the self-assembly process by which native proteins convert into insoluble fibrillar structures, has varied implications in human health, biotechnology and material science like influencing the yield of protein expression or to be involved with a class of late-onset and slow-progressing diseases like Alzheimer’s, Parkinson 's. Deciphering the code of protein self-organization process resulting into aggregation has been an intellectual challenge for scientists over the past few decades. Active research in this field and many recent advances in physical techniques along with molecular dynamics simulation over the past few years have significantly increased our understanding of the initial driving forces
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Stirring as an agitation method is therefore quite useful in kinetic studies as process of aggregation without agitation can sometime take several days to months for completion. Table 1.2 describe this effect of agitation on aggregation process of various proteins, clearly showing the drastic change in kinetic parameters like lag time in absence and presence of agitation condition like stirring. Such agitation could possibly induce cavitation, local thermal effects and/or interfacial effects involving rapid transportation of either aggregated or adsorbed species from the interface into solution. Bolder et al. in their study on whey protein have speculated that stirring may also be breaking the immature fibrils leading to production of more active fibrils. But the mechanism of how aggregation process gets speed up on stirring is hitherto unclear.
In this study, we have tried to unravel the effects of stirring on protein aggregation process, especially on the early events during the lag phase of the kinetic profile which governs the rate and morphological developments of final aggregates. Over the past decades, most of the biophysical research has been directed towards later phase of aggregation especially about the structure of mature fibril and on possible oligomeric toxic
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