This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Structure and dynamics study of cutdomain protein using NMR. The cutdomain protein is a member of important family of DNA-binding proteins. Research in the field of macromolecule structure has progressed very rapidly. X-ray diffraction techniques have been successfully used to study the crystal structure of number of macromolecules, but methods to determine solution structures of macromolecules had previously been limited. Recent technical improvements in high resolution NMR spectroscopy combined with molecular biology techniques provide powerful tools to study the structure and dynamics of macromolecules. Since NMR is very sensitive to local conformational changes and gives direct information on the tertiary structure and dynamics of macromolecules in solution, it plays an increasingly important role in these studies. A focus of this laboratory involves studies of protein-nucleic acid interactions by a combination of NMR and biochemical techniques. NMR is used to study the structure and dynamics of both the free protein and the protein-nucleic acid complex. The biochemical techniques are used to relate the structure to its function.
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