{"id":{"repo_id":"mit","oai_identifier":"oai:dspace.mit.edu:1721.1/112903"},"canonical_url":"https://search.dev.ndltd.org/etd/mit/oai:dspace.mit.edu:1721.1/112903","repository":{"repo_id":"mit","name":"MIT","base_url":"https://dspace.mit.edu/oai/request"},"display":{"title":"Protein potentials and domains : re-use and composability","abstract":"Protein-protein interactions are one of the cornerstones of biological processes throughout the cell. Unfortunately, lack of available data precludes many possible approaches to modeling these fundamental interactions at scale. This thesis focuses on a specific set of protein domains, known as peptide-binding domains (PBD), that play a particularly crucial role in mediating protein-protein interactions. Using these components as a basis, we develop a model for protein-protein interactions driven by PBDs. Our approach revises a previously proposed model, both expanding its applicability to a much larger set of PBDs and improving the performance of the model. We conclude with an application of our model that shows the flexibility of our approach.","abstract_html":"Protein-protein interactions are one of the cornerstones of biological processes throughout the cell. Unfortunately, lack of available data precludes many possible approaches to modeling these fundamental interactions at scale. This thesis focuses on a specific set of protein domains, known as peptide-binding domains (PBD), that play a particularly crucial role in mediating protein-protein interactions. Using these components as a basis, we develop a model for protein-protein interactions driven by PBDs. Our approach revises a previously proposed model, both expanding its applicability to a much larger set of PBDs and improving the performance of the model. 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