Dept. of Chemical Sciences
Tata Institute of Fundamental Research
Mumbai
India
maiti@tifr.res.in
When proteins fold, they choose the biologically appropriate conformation from an astronomical number of possibilities. It turns out that for a class of human proteins, alternate aggregation-prone conformations are energetically accessible. Sometimes the protein molecules migrate to these other conformations, with disastrous consequences, causing diseases such as Alzheimer's and Parkinson's. With single molecule level fluorescence spectroscopy, we are trying to understand the conformational energy landscape that governs this change, identify the dominant intermediates during the aggregation process, and correlate this information with relevant clinical and biological findings.