Direct Force Measurements

The ability to measure directly forces between biopolymers in macroscopic condensed arrays has greatly changed our understanding of how molecules interact at close spacings, the last 10-15 Angstroms separation. The universality of the force characteristics observed for a wide variety of macromolecules, including DNA, proteins, lipid bilayers, and carbohydrates, has led us to conclude that the energy associated with structuring water between close surfaces dominates intermolecular forces. We are currently focusing on understanding the connection between hydration force magnitudes and the chemical natures of the interacting surfaces. -- Selected references

Hydration Changes Linked to Sequence Specific DNA-Protein Recognition Reactions

Our ultimate goal is to apply the lessons from direct force measurements to the recognition reactions that control cellular processes. We in particular are focusing on differences in water sequestered by complexes of four sequence specific DNA binding proteins with varying DNA sequences, with particular emphasis on correlating binding energy and water incorporated and on the energy necessary to remove hydrating water from complexes. -- Selected references