General
Dr. Samrat Mukhopadhyay
IISER, Mohali
<span style="\\"color:" rgb(0,="" 0,="" 0);="" font-family:="" \\"times="" new="" roman\\";="" font-size:="" medium;\\"="">Water molecules residing in the hydration layer at the protein-water interface of globular proteins exhibit unique dielectric and dynamical characteristics that are fundamentally different from bulk water. These dynamically restrained water molecules in the hydration layer of proteins are termed as "Biological Water" and play a critical role in the folding, enzyme catalysis, protein-DNA and protein-protein interactions, and amyloid formation. Protein misfolding and aggregation resulting in amyloid formation are associated with a variety of debilitating human disease such as Alzheimer’s, Parkinson’s and transmissible prion diseases, systemic amyloidosis and cancer. My laboratory at IISER Mohali has been addressing some important structural, dynamical, nanoscopic and mechanistic issues of an emerging class of amyloid-forming proteins known as Intrinsically Disordered Proteins (IDPs). IDPs challenge the traditional sequence-structure-function paradigm and are associated with important functions and amyloid diseases. Using a diverse array of biophysical and biochemical techniques, we have previously shown how these proteins undergo a disorder-to-order transition during amyloid formation. Recently, using femtosecond time-resolved fluorescence spectroscopy, we have embarked upon studies aimed at unraveling the intriguing role of water molecules in the conformational transition and aggregation of disease-related IDPs. I will discuss our recent ultrafast spectroscopy results that illuminate the intriguing behavior of water molecules in these proteins and reveal a novel mechanistic aspect of aberrant protein aggregation.
