BioE Professor Jeffrey Ruberti (co-PI) along with bioengineering affiliated and College of Science faculty, including Professor Mark Williams (PI), and Associate Professors Penny Beuning (co-PI), Meni Wanunu (co-PI), and Ke Zhang (co-PI) were awarded a $1M NSF grant for the "Acquisition of a Lumick's SuperC-TRAP correlative optical tweezers and fluorescence microscope (CTFM) system."
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- M. Nabuan Naufer, D.A. Murison, I. Rouzina, P.J. Beuning, M.C. Williams, Single-Molecule Mechanochemical Characterization of E. coli Pol III Core Catalytic Activity, Protein Science, 26, 2017, 1413-1426
- K. Posty, E.D. Olson, M. Nabuan Naufer, R.J. Gorelick, I. Rouzina, M.C. Williams, K. Musier-Forsysth, J.G. Levin, Mechanistic Differences Between HIV-1 and SIV Nucleocapsid Proteins and Cross-Species HIV-1 Genomic RNA Recognition, Retrovirology, 13(89), 2016
- A.A. Almaqwashi, T. Paramanathan, I. Rouzina, M.C. Williams, Mechanisms of Small Molecule–DNA Interactions Probed by Single-Molecule Force Spectroscopy, Nucleic Acids Research, 44(9), 2016, 3971-3988
- A.A. Almaqwashi, J. Andersson, P. Lincoln, I. Rouzina, F. Westerlund, M.C. Williams, Dissecting the Dynamic Pathways of Stereoselective DNA Threading Intercalation, Biophysical Journal, 110(6), 2016, 1255-1263
- M.J. McCauley, I. Rouzina, K.A. Manthei, R.J. Gorelick, K. Musier-Forsyth, M.C. Williams, Targeted Binding of Nucleocapsid Protein Transforms the Folding Landscape of HIV-1 TAR RNA, Proceedings of the National Academy of Sciences, 112(44), 2015, 13555-13560
- K.R. Chaurasiya, M.J. McCauley, M.C. Williams, et al., Oligomerization Transforms Human APOBEC3G from an Efficient Enzyme to a Slowly Dissociating Nucleic Acid-binding Protein, Nature Chemistry, 6, 2014, 28-33
- H. Wu, M. Mitra, K. Musier-Forsyth, M.C. Williams, et al., Aromatic Residue Mutations Reveal Direct Correlation Between HIV-1 Nucleocapsid Protein’s Nucleic Acid Chaperone Activity and Retroviral Replication, Virus Research, 171, 2013, 263-277
Prof. Williams’ main research interest is the biophysics of DNA-protein interactions. DNA is normally found as a double helix consisting of a sequence of base pairs, representing the genetic code. In order for this code to be read to create proteins (transcription and translation) or to make copies of the DNA (replication), the two strands of the double helix must be separated to expose the bases. The processes of replication and transcription are regulated by proteins that bind to DNA and alter the stability of the double helix. In his research Prof. Williams uses optical tweezers instruments to apply very small forces to single DNA molecules. Measurement of these forces allows him to determine the stability of the DNA double helix and the extent to which various DNA binding proteins alter the structure and stability of DNA. This approach provides unique insights into the function of these proteins in the cell.
Ph.D., University of Minnesota, 1998