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Bill Broadhurst is a researcher in the Department of Biochemistry, focusing on the structural dynamics of modular polyketide synthases (PKSs), which are the largest integrated enzyme complexes known. His research explores how these complexes, which are organized into clusters of catalytic domains, produce bioactive products like antibiotics and toxins. His work involves examining the global conformational changes and transient interfaces that control the growth of polyketide chains. Broadhurst's key investigations have identified the roles of acyl carrier protein domains that serve as attachment points during the growing substrate chain's shuttling to the active site. He studies specific protein-protein interactions and the recognition required for the release of final polyketide products. His findings have important implications for the engineering of modified PKS systems to create novel compounds. His research goals include exploring the quaternary structure rearrangement of PKS modules, the influence of ACP domain structure on PKS programming, and the application of bioinformatics tools to predict structures of new natural products from environmental DNA.
Standard postgraduate requirements for Department of Politics and International Studies (POLIS) and related humanities departments.