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The scientists working in the Laboratory of Physical and Structural Biology (LPSB) are mostly physicists who are ready to learn about biology and chemistry. As such, we have adopted a perspective that differs from that of our biologist and chemist colleagues. To us, electrical "noise" from an ionic channel shows molecular dynamics while charge patterns on macromolecules create precision-fit helices, and DNA at its densities in a virus reveals a liquid-crystal.
The next step in structural biology is not simply to determine the structure of every identifiable entity from molecule to organelle but rather to learn how structures work through the physics and chemistry of the intermolecular forces that drive them. We can then learn from the increasing number of protein, nucleic acid, saccharide, and lipid structures how to design agents that compete effectively with deviant interactions associated with disease.
During this past year, members of the LPSB have been able to watch and time the passage of an antibiotic moving through a bacterial transmembrane ionic channel; show how solution conditions modify the specific versus nonspecific binding of proteins to DNA; prove that the bone protein collagen in its monomer form actually denatures at body temperatures; and formulate the mechanical strength of DNA to predict the consequences of various solutes in single-molecule stretching experiments.