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Scientific Resources
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