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Mark
Williams
Associate Professor
PhD University of Minnesota, 1998
(617)373-7323
ma.williams@neu.edu
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Research
Summary:
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.
Recent Publications:
1. Mark C. Williams. Stuffing a virus with DNA: Dissecting viral genome packaging (Commentary). Proceedings of the National Academy of Sciences USA 104: 11125-11126 (2007).
2. Ioana D. Vladescu, Micah J. McCauley, Megan E. Nuņez, Ioulia Rouzina, and Mark C. Williams. Quantifying force-dependent and zero-force DNA intercalation by single-molecule stretching. Nature Methods 4: 517-522 (2007).
3. Micah J. McCauley and Mark C. Williams. Mechanisms of DNA Binding Determined in Optical Tweezers Experiments. Biopolymers 85: 154-168 (2007).
4. Leila Shokri, Boriana Marintcheva, Charles C. Richardson, Ioulia Rouzina, and Mark C. Williams. Single molecule force spectroscopy of salt-dependent bacteriophage T7 gene 2.5 protein binding to single-stranded DNA. Journal of Biological Chemistry 281: 38689-38696 (2006).
5. Margareta Cruceanu, Robert J. Gorelick, Karin Musier-Forsyth, Ioulia Rouzina, and Mark C. Williams. Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function. Journal of Molecular Biology 363: 867-877 (2006).
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