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020    9780549477365 
035    (UMI)AAI3302194 
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100 1  Amero, Carlos Daniel 
245 10 Protein function study by NMR spectroscopy 
300    243 p 
500    Source: Dissertation Abstracts International, Volume: 69-
       02, Section: B, page: 0876 
500    Adviser: Mark Foster 
502    Thesis (Ph.D.)--The Ohio State University, 2008 
520    It is essential to understand how proteins perform their 
       work and how they interact with other molecules. We have 
       used Nuclear Magnetic Resonance (NMR) spectroscopy to 
       study structure, dynamics and interactions in several 
       systems: Poliovirus 3C protein, Cre recombinase, an 
       archaeal RNase P protein (Rpp21) and Peptide Deformylase 
       (PDF). This dissertation discusses these different 
       biological systems in separated chapters. Chapter 1 serves
       as an introduction to the basics of Protein NMR 
520    Chapter 2 involves analysis of RNA interactions with the 
       poliovirus 3C protein. Replication of picornaviral genomes
       requires recognition and binding by the virus-encoded 3C 
       protein of at least three RNA elements. We have used 
       chemical shift mapping to provide unique site-specific 
       insight into residues of 3C that interact with RNA, and 
       set the stage for detailed structural investigation of the
       3C-RNA complex by NMR 
520    Chapter 3 is devoted to Cre recombinase from bacteriophage
       P. This enzyme recognizes specific DNA sequences on two 
       DNA strands and mediates recombination between these sites
       via the formation of a covalent protein-DNA complex and a 
       Holliday junction intermediate. We have used heteronuclear
       NMR methods to obtain insights into the free structure, 
       dynamics and interaction with DNA 
520    Chapter 4 focuses in RNase P, the ubiquitous 
       ribonucleoprotein enzyme responsible for cleaving the 5'-
       leader sequence of precursor tRNA (pre-tRNA) molecules 
       during maturation. We have determined the solution 
       structure of the Rpp21 protein from the hyperthermophilic 
       archaeon, Pyrococcus furiosus (Pfu) using conventional and
       paramagnetic NMR techniques and characterize the 
       interaction of Rpp21 with Pfu  Rpp29 
520    Chapter 5. Peptide deformylase (PDF) is an enzyme that is 
       responsible for removing the formyl group from nascently 
       synthesized polypeptides in bacteria. It has attracted 
       much recent attention as a potential target for novel 
       antibacterial agents. We used 15N NMR spectroscopy and 
       isothermal titration calorimetry to investigate the high-
       affinity interaction of PDF with actinonin, a naturally 
       occurring potent PDF inhibitor. The results of these 
       studies improve our understanding of the thermodynamic 
       global minimum and has potentially important implications 
       for structure-based design of protein-binding ligands 
590    School code: 0168 
590    DDC 
650  4 Biophysics, General 
690    0786 
710 2  The Ohio State University 
773 0  |tDissertation Abstracts International|g69-02B 
856 40 |u