J. Lawrence Oncley Collegiate Professor of Chemistry and Biophysics
Dr. Al-Hashimi is J. Lawrence Oncley Collegiate Professor of Chemistry and Biophysics Professor at the University of Michigan. He received his doctorate in Biophysical Chemistry from Yale University in 2000 for research on the development of residual dipolar coupling NMR methods to study the structure and dynamics of proteins. Between 2000-2002, Dr. Al-Hashimi was a Research fellow, Research Associate, and Senior Research Scientist at the Memorial Sloane-Kettering Cancer Center in NYC, where he developed and applied NMR methodology to study the structure and dynamics of nucleic acids. Now at the University of Michigan, the Al-Hashimi laboratory is focused on the development and application of NMR and computational methods to visualize dynamic biological processes at the atomic level within living cells and to develop a fundamental biophysical understanding to aid the design of therapeutics. He is the recipient of the National Science Foundation Career Award, LSA Excellence in Teaching Award, Ralph E. Powe Junior Faculty Enhancement Award, and the Founder’s Medal. His work on molecular visualization and nucleic acid dynamics was recognized by Popular Science Magazine, which listed him among the 'Brilliant 10' scientists and engineers in USA (2011). In 2009, he co-founded Nymiurm Inc, which is a start-up biotech company that is using the methods developed in the Al-Hashimi lab to increase the pace of RNA-targeted drug discovery.
Currently, we cannot experimentally see biomolecules preforming their cellular functions – such as DNA replication and protein catalysis – at atomic resolution. Our group is developing methods that combine powerful Nuclear Magnetic Resonance (NMR) experiments with computational approaches – that make it possible to visualize the dynamics of biomolecules at atomic resolution. These atomic "movies" are allowing us to understand some of the most curious aspects of biomolecule behavior, such as how they change structure in a specific manner, make new discoveries that redefine the iconic DNA double helix, and also enabling biotechnological applications, such as RNA-targeted drug discovery
77. Nikolova, E, Bascom, G., Andricioaei, I, Al-Hashimi, H. M. Probing Sequence-specific DNA Flexibility in A-tracts and Pyrimidine-purine Steps by NMR 13C Relaxation and MD Simulations. Biochemistry, In Press
76. Dethoff, L.1, Petzold, K.1, Chugh, J.1, Casiano-Negroni, A., and Al-Hashimi, H. M. Visualizing Transient Low-Populated Structures of RNA Nature In Press 1Co-first authors
75. Bothe, J., Lowenhaupt, K., and Al-Hashimi, H. M. Incorporation of CC Steps into Z-DNA: Interplay Between B/Z Junction and Z-DNA Helical Formation Biochemistry, 51(34):6871-9 2012.
74. Prevette, L. Nikolova, E., Al-Hashimi, H. M., and Banaszak Holl, M. Intrinsic Dynamics of DNA-Polymer Complexes: A Mechanism for DNA Release. Mol. Pharm, Molecular Pharmaceutics, 9(9):2743-9 2012.
73. Eichhorn, C.D., Yang, S., and Al-Hashimi, H.M. Characterizing RNA Dynamics using NMR Residual Dipolar Couplings, in Recent Developments in Biomolecular NMR, Royal Society of Chemistry Publishing, Cambridge, 2012.
72. Nikolova, E. N., Gottardo, F. L. and Al-Hashimi, H. M. Probing Transient Hoogsteen Hydrogen Bonds in Canonical Duplex DNA using NMR Relaxation Dispersion and Single-atom Substitution. J. Am. Chem. Soc., 134(8): 3667-70 2012.
71. Dethoff, E. A., Chugh, J., Mustoe, A. M. and Al-Hashimi, H. M. Functional Complexity and Regulation through RNA Dynamics. Nature,482(7385):322-330 2012
70. Eichhorn, C. D., Feng, J., Suddala, K. C., Walter, N. G., Brooks, C. L. and Al-Hashimi, H. M. Unraveling the Structural Complexity in a Single Stranded RNA Tail: Implications for Efficient Ligand Binding in the Prequeuosine Riboswitch. Nucleic Acids Res., 40(3): 1345-55 2012 (Featured article).
69. Mustoe, A. M., Bailor M. H., Teixeira, R., Brooks, C. L. and Al-Hashimi, H. M. New Insights Into the Fundamental Role of Topological Constraints as a Determinant of Two-Way Junction Conformation. Nucleic Acids Res., 40(2): 892-904 2012.