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Peter Flynn

assistant Professor of chemistry

B.S. University of Oregon

Ph.D. University of Washington

Research

References

pfflynn@chem.utah.edu

Peter Flynn's Lab Page

Research

Research efforts in the Flynn group emphasize biophysical characterization of biologically important macromolecules. Our approach combines multidimensional, multinuclear solution NMR methods with fluorescence, calorimetry and surface plasmon resonance to generate a detailed characterization of structure and function.

Structural and Dynamic Origins of RNA Processing. The catalytic activity of the spliceosome arises from a complex orchestration of interactions among proteins, RNA oligomers and the pre-mRNA, according to a specific time-order, leading to excision of introns.   Model systems currently being studied in the lab involves the interaction between kink-turn binding proteins (15.5kD protein, Snu13p, L7) and their RNA target oligomers.   The 15.5K/Snu13p class of K-turn binding proteins have recently been shown to have dual functional roles in RNA processing - these proteins are involved in nuclear (pre-mRNA) splicing and also participate in methylation and pseudouridylation of RNA molecules.   Efforts to characterize structure and biophysical properties of these molecules will allow us to elucidate the physical basis of recognition and specificity in these important systems.

Transcription Control of Tryptophan Biosynthesis in Bacteria. RNA antiterminator sequences (RATs) represent an essential transcriptional and translational control element in a number of biological systems.   In the presence of high levels of tryptophan a toroidal B subtilis protein named TRAP (trp-RNA-binding attenuator protein) binds the RAT of the trp-operon with high affinity, whereas at low levels of tryptophan the interaction is much weaker.   This distinction leads to highly effective expression-level control of tryptophan biosythesis.   As in studies of the K-turn binding protein-RNA interactions, our goal is to elucidate the fundamental features of the interaction using a combination of structural and biophysical methods.

Encapsulation of Macromolecules.   Proteins, nucleic acid oligomers and other biologically important macromolecules that are normally found in aqueous solution may be encapsulated within a surfactant shell (i.e., dioctyl sulfosuccinate) and transported into non-native solvent systems (i.e., n-alkanes, C 3 H 5 - C 5 H 12 ). This novel approach opens up new opportunities for solution NMR studies of larger macromolecules as well as fundamental studies of chemical physics using concise, precisely defined environments.   Current group effort are focused on the development of encapsulation as a novel method for investigating proteins under novel conditions, e.g., at low temperature and in crowded environments.

Macromolecular Dynamics. The importance of internal dynamics in proteins as a factor in characterizing function has become increasingly apparent, and solution NMR methods are particularly well-suited to evaluate such effects.   Studies of backbone dynamics in proteins indicate that the main-chain atoms are generally highly and homogeneously ordered whereas studies of side-chain motion suggest a more heterogeneous picture.   We are particularly interested in probing dynamics at the interfaces between components of protein-protein and protein-RNA complexes, across a wide range of time scales (from microseconds to hours) to characterize the full range of motions that influence the interaction.   New efforts target characterization of dynamics in the RNA oligos, which promises to generate novel insights into the physical nature of protein-RNA recognition events.

References