Single Molecule Studies of DNA Interactions
The main research interest of the Williams lab 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 our research we use optical tweezers instruments to apply very small forces to single DNA molecules. Measurement of these forces allows us 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.
|News highlight:||Interview with Professor Williams in NEU College of Science Newsletter|
|Retroviral and retrotransposon replication interactions - single molecule analysis of nucleic-acid protein interactions involved in replication of retroviruses such as HIV-1 and retrotransposons such as LINE1, as well as human innate immune proteins that give resistance to retroviruses|
|E. coli replication interactions - single molecule studies of polymerases and accessory proteins involved in E. coli DNA replication and repair|
|Nucleosome accessibility in eukaryotic systems - single molecule studies of nucleosome-associated proteins such as HMGB architectural DNA bending proteins, including studies of nucleosome stability.|
Small molecule interactions with DNA - detailed characterization of the energy landscape of small molecule-DNA interactions to optimize characteritics for potential anti-cancer drugs.