We devote a part of our efforts to the development of improved NMR techniques and hardware, as well as protein engineering. We are continuing and expanding our efforts to develop new approaches to tagging macromolecules with paramagnetic centers and obtaining unique structural information about intermolecular interactions and structures of multi-component complexes. In addition, new approaches are developed when traditional methods require augmentation with new experiments or data. These methods include novel isotopic labeling schemes, pulse sequence development, automated methods and novel methods in relaxation NMR of proteins. This effort is continuing as a subset of the various structural biology projects described in other parts of the annual report. Specific developments have included the use of non-uniform sampling to speed up data acquisition of multi-dimensional NMR data, tagging with a range of molecules to facilitate both paramagnetic relaxation enhancement and the anticipated use of pulsed EPR (DEER) to measure long-range distances in multi-component complexes. Ongoing work in membrane mimetics is expected to impact both major projects in the lab in the coming year and beyond.
| Chao, Fa-An; Byrd, R Andrew (2017) Application of geometric approximation to the CPMG experiment: Two- and three-site exchange. J Magn Reson 277:8-14 |
| Chao, Fa-An; Byrd, R Andrew (2016) Geometric Approximation: A New Computational Approach To Characterize Protein Dynamics from NMR Adiabatic Relaxation Dispersion Experiments. J Am Chem Soc 138:7337-45 |
| Gill, Michelle L; Byrd, R Andrew; Palmer III, Arthur G (2016) Dynamics of GCN4 facilitate DNA interaction: a model-free analysis of an intrinsically disordered region. Phys Chem Chem Phys 18:5839-49 |
| Sun, Shangjin; Gill, Michelle; Li, Yifei et al. (2015) Efficient and generalized processing of multidimensional NUS NMR data: the NESTA algorithm and comparison of regularization terms. J Biomol NMR 62:105-117 |
| Fang, Xianyang; Wang, Jinbu; O'Carroll, Ina P et al. (2013) An unusual topological structure of the HIV-1 Rev response element. Cell 155:594-605 |
