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Donald Hamelberg

Professor; Associate Chair; Graduate Director

Georgia State University, Ph.D. (2001)
University of Illinois, Chicago, Postdoctoral Research Fellow (2001-2003)
Howard Hughes Medical Institute and University of California, San Diego, Postdoctoral Research Fellow (2003-2005)


Computational Chemistry, Biophysical Chemistry


Research Interests:

The research in our group focuses on the application and development of theoretical and computational methods with the intent of gaining an in-depth understanding of biomolecular switches. Intricate networks of interacting proteins and RNAs mediate many interactions in cell signaling pathways. Deregulation of these pathways could trigger cellular transformation, oncogenesis, and a host of other diseases. The research in our lab seeks to decipher the underlying principles governing cell signaling mechanisms and biomolecular interactions involving proteins and RNAs. In these endeavors, we use simulation-based approaches, and related statistical mechanics, classical and quantum mechanical methods, as a complementary tool to experiments.


Recent publications:
1. Ho K. C., Hamelberg D., (2016). Oscillatory Diffusion and Second-Order Cyclostationarity in Alanine Tripeptide from Molecular Dynamics Simulation. Journal of Chemical Theory and Computation, 12, 372–382
2. Barman A., Batiste B., Hamelberg D., (2015). Pushing the Limits of a Molecular Mechanics Force Field To Probe Weak CH-pi Interactions in Proteins. Journal of Chemical Theory and Computation, 11, 1854-1863
3. Velazquez H. A., Hamelberg D., (2015). Dynamical role of phosphorylation on serine/threonine-proline Pin1 substrates from constant force molecular dynamics simulations. Journal of Chemical Physics, 142, 075102
4. Doshi U., Hamelberg D., (2015). Towards fast, rigorous and efficient conformational sampling of biomolecules: advances in Accelerated Molecular Dynamics. Biochimica et Biophysica Acta (BBA) – General Subjects, 1850, 878-888
5. Barman A., Hamelberg D., (2015). Loss of intramolecular electrostatic interactions and limited conformational ensemble may promote self-association of cis–tau peptide. Proteins: Structure, Function, and Bioinformatics, 83, 436–444

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