NMR spectroscopy based analysis of protein structure and function
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Nuclear magnetic resonance (NMR) has become one of the most common methods for the determination of three-dimensional (3D) solution structures of proteins. On the other hand, bioinformaticians provide powerful tools to study a protein's biological role. The work of this thesis consists of two major parts: (1) the NMR structure determination of the Northeast Structural Genomics Consortium target protein Xanthomonas campestris Xcc2852, and (2) the functional annotation of the NESG Consortium target protein Escherichia coli yhgG. For the 3D structure determination in part (1), we used a standard protocol for NMR-based structural genomics, which enables one to rapidly collect and analyze NMR data. A set of G-matrix Fourier Transform (GFT) NMR experiments were used and feasibility and robustness of the protocol is exemplified. In the bioinformatics study of part (2), sophisticated sequence and structure alignment algorithms were used to explore the possible function of target protein yhgG.