Adjunct Associate Professor of Chemistry
B.S. University of Oregon
Ph.D. University of Washington
Peter Flynn's Lab Page
Peter Flynn's PubMed Literature Search
Biological Chemistry Program
Biological NMR and Biophysics
Research efforts in the Flynn group emphasizes biophysical characterization of biologically
active macromolecules using multidimensional/multinuclear solution NMR methods. Our
approach emphasizes development of in vitro models of the cellular environment, and
explores the influence of crowded environments on the behavior of proteins and small
RNA oligonucleotide model systems.
Encapsulation of Macromolecules. Proteins, nucleic acid oligomers, and other biologically important macromolecules may be encapsulated within a surfactant shell (i.e., dioctyl sulfosuccinate) and transported into non-native solvent systems (i.e., short-chain n-alkanes). This novel approach opens up new opportunities for solution NMR studies of larger macromolecules, as well as providing a unique and powerful new approach to studies of the environment on the physical behavior of macromolecules. Current group efforts are focused on the development of encapsulation as model of the crowded intracellular environment.
Macromolecular Structure and Dynamics. All biological function derives from the structure and dynamics of macromolecules. Structure has long been used as the primary lead in efforts to understand the molecular basis of function, and remains fundamentally important. 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 motion 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..
Figure One: Micelle Model
Figure Two: Schematic Diagram of Encapsulation of an RNA Oligonucleotide
Figure Three: Solution Structure of 15.5K Protein
- Workman H, Flynn PF (2009) Stabilization of RNA oligomers though reverse micelle encapsulation. J. Am. Chem. Soc. 131:3806-3807
- Workman H, Skalicky JJ, Flynn PF (2008) 1H, 13C, and 15N Backbone and Side Chain Resonance Assignments for the RNA-binding protein Snu13p from Saccharomyces cerevisiae. J. Biomol. Assign. 2:1-3
- Van Horn WD, Ogilvie ME, Flynn PF (2008) Use of Reverse Micelles in Membrane Protein Structural Biology. J. Biolmol. NMR 40:203-211
- Workman H, Skalicky J, Flynn PF (2007) 1H, 13C, and 15N Backbone and Side Chain Resonance Assignments for the RNA-binding protein Snu13p from Saccharomyces cerevisiae. Published online 12/4/2007 in Biomolecular NMR Assignments.
- Soss SE, Flynn PF (2007) Functional Implications for a Prototypical K-turn Binding Protein from Structural and Dynamical Studies of 15.5K. Biochemistry 46:14979-14986
- Soss SE, Flynn PF (2007) NMR Assignment of the Human Spliceosomal 15.5K Protein. J. Biomol. NMR. 38:175
- Simorellis AK, Flynn PF (2006) Fast Local Backbone Dynamics of Encapsulated Ubiquitin. J. Am. Chem. Soc. 128:9580-9581
- Simorellis AK, Van Horn WD, Flynn PF (2006) Dynamics of Low Temperature Water Shedding from Reverse Micelles. J. Am. Chem. Soc. 128:5082-5090
- Van Horn WD, Simorellis AK, Flynn PF (2005) Low Temperature Studies of Encapsulated Proteins. J. Am. Chem. Soc. 127:13553-13560
- Simorellis AK, Flynn PF (2004) A Pulsed Field Gradient NMR Experiment for Translational Diffusion Measurements in Low Viscosity Hydrocarbon Solvents. J. Magn. Reson. 170:322-328