Exploring the structure and dynamics fo proteins in non-native states using fluorescence spectroscopy
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In the present thesis, structure and dynamics of non-native states in proteins are discussed under different experimental conditions. Owing to their conformation heterogeneity their involvement in protein folding pathway including their role in different protein misfolding diseases, non-native forms of protein are important both for basic and applied areas of biological science. Local structures in protein under extreme denaturing conditions are known as residual structures and are believed to act as nucleation site for protein folding events. Locating these structures are important to reveal protein folding/unfolding events. I used fluorescence from trp(s) as a simple and sensitive tool to hunt for these structures in different proteins, namely, barstar, subtilisin carlsberg (SC), human serum albumin (HSA), melittin, myelin basic protein (MBP), glucagon, Ribonuclease T1 (RNase T1), Trp-Met-Asp-Phe, bovine serum albumin (BSA) and hen egg white lysozyme (HEWL) after nightlong (~12 hours) incubation in 6 M GdnCl at room temperature. Except BSA and HEWL all other proteins used here contain single trp per polypeptide chain..
Supervisor: R. Swaminathan
BIOSCIENCES AND BIOENGINEERING