Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/30223
Title: Understanding protein structures- function relationship by NMR Spectroscopy
Authors: LIM JACK WEE
Keywords: Protein, NMR Spectroscopy, Midkine, Acyl Carrier Protein, Transcriptional Repression Domain, Structure-Function
Issue Date: 19-Aug-2011
Source: LIM JACK WEE (2011-08-19). Understanding protein structures- function relationship by NMR Spectroscopy. ScholarBank@NUS Repository.
Abstract: NMR spectroscopy is a gentle yet powerful tool to study different proteins. Here we will present and characterize three types of proteins: midkine (Mdk), acyl carrier protein (ACP) and a transcriptional repression domain (TRD) primarily by NMR spectroscopy. For Mdk, we will first explore the novel role of a highly conserved basic hinge for proper heparin binding and embryogenesis. Further we construct Gly7x-hinge mutants to backup our findings. Next we will present the first ACP domain (meACP) structure from a highly reducing type I iterative polyketide synthase CalE8, featuring a distinct hydrophobic patch and an acidic patch embodying a non-canonical three-helix bundle. In addition, NMR titrations further suggest that meACP interacts with its thioesterase partner CalE7 via its meACP-tethered polyene moiety. Lastly, we will characterize TRD from the methyl-CpG binding domain 1 (MBD1) family. Surprisingly TRD is highly unstructured yet crucial for MBD1 function.
URI: http://scholarbank.nus.edu.sg/handle/10635/30223
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