{"id":{"repo_id":"nus","oai_identifier":"oai:scholarbank.nus.edu.sg:10635/216496"},"canonical_url":"https://search.dev.ndltd.org/etd/nus/oai:scholarbank.nus.edu.sg:10635/216496","repository":{"repo_id":"nus","name":"National University of Singapore","base_url":"https://scholarbank.nus.edu.sg/oai/request"},"display":{"title":"STRUCTURE, FUNCTION AND FOLDING OF THREE FINGER TOXINS","abstract":"Three finger toxins (3FTxs) are one of the family of peptides in snake venom. Despite the common protein fold, they exhibit diverse pharmacological activities. Our group characterized Oh9-1, a neurotoxin from venom of Ophiophagus hannah. Although Oh9-1 binds to the same acetylcholine binding pocket as the -neurotoxins, it lacks key functional residues. In this thesis, I describe the three-dimensional structure of Oh9-1 by NMR. Unlike the above class of postsynaptic neurotoxins, we identified a 3FTx that acts at the presynaptic site. This toxin, isolated from venom of Micrurus fulvius, was named as “presynapsin”. Systemic sequence investigation was done to understand the functional diversity. Finally, I attempted to determine the structural elements that assist in the native disulphide pairings which help in maintaining the canonical 3FTx-fold. I have evaluated the role of primary sequence and secondary structures to define the molecular determinants that govern the disulphide pairing.","abstract_html":"Three finger toxins (3FTxs) are one of the family of peptides in snake venom. Despite the common protein fold, they exhibit diverse pharmacological activities. Our group characterized Oh9-1, a neurotoxin from venom of Ophiophagus hannah. Although Oh9-1 binds to the same acetylcholine binding pocket as the -neurotoxins, it lacks key functional residues. In this thesis, I describe the three-dimensional structure of Oh9-1 by NMR. Unlike the above class of postsynaptic neurotoxins, we identified a 3FTx that acts at the presynaptic site. This toxin, isolated from venom of Micrurus fulvius, was named as “presynapsin”. Systemic sequence investigation was done to understand the functional diversity. Finally, I attempted to determine the structural elements that assist in the native disulphide pairings which help in maintaining the canonical 3FTx-fold. 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