Our laboratory has been investigating the mechanistic details of how a protein attains its functional three dimensional structure. We are also studying the conformational and other factors which contribute to the alteration of folding pathways leading to aggregation. The problems of protein mis-folding and aggregation, which have serious implications in a number of neurodegenerative diseases, are difficult to study. This is because; the folding and aggregation landscape is inherently heterogeneous, consisting of multiple pathways. Since the traditional biochemical and biophysical techniques require an optimum concentration of aggregated molecules for their detection, monitoring the early stages is difficult. Our lab has been using sensitive fluorescence methods, which can provide single molecule resolution, to address these problems. In this talk, we would discuss some of these data, which have been obtained using a number of relevant model proteins.
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