Structural Basis of Transfer Ribonucleic Acid Function

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The nature and rate of conformational changes that take place in transfer RNA (tRNA) as it interacts with the macromolecular components involved in protein synthesis remain unclear. Nuclear magnetic resonance (NMR) is a powerful, non-destructive method for studying the structure, conformation and dynamic properties of tRNA in solution. While most NMR studies have involved protein NMR, F-19 NMR offers the advantages of high sensitivity to detection, a large range of chemical shifts and great sensitivity to the environment of the nucleus. Dr. Horowitz is using high resolution F-19 NMR to probe conformational changes in 5-fluorouracil (FUra)-substituted E. coli tRNAs as they relate to function. Interpretation of results at the molecular level requires reliable peak assignments; approximately half the resonances in the F-19 NMR spectrum of the valine tRNA have been assigned. This project will be expanded to include experiments with molecular fragments and hybrid tRNA molecules, chemical modification studies and the investigation of tRNAs with specific FUra residues replaced with other bases by recombinant DNA techniques. Then will be used in assigning the remaining peaks in the F-19 spectrum.