Self-organization, molecular mechanics, and catalytic functions of nucleoprotein complexes studied using single-DNA micromanipulation

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This project focuses on the study of DNA-protein complexes through single-DNA micromanipulation. Using magnetic tweezers and micropipette manipulation of DNAs attached to micron-sized particles, the dynamics of formation, mechanical properties, and catalytic function of nucleoprotein complexes will be measured. Self-assembly, activities and disassembly of these protein-DNA complexes will be studied via precise time-resolved measurement of mechanical properties, i.e. molecular lengths as a function of applied force. This simple yet versatile approach allows observation of kinetics of reactions as well as equilibrium states, for proteins that reorganize DNA structure. The project will also include development of transverse magnetic tweezer methods, including techniques for experiments on two DNA segments at once. Broader impacts of this research will be via its highly interdisciplinary nature, and by development of new biophysical techniques (transverse magnetic tweezer and combined magnetic tweezer/micropipette methods) for study of DNA-protein interactions. Along with this, the proposed activities will focus on research education for Ph.D. and postdoctoral students, combining physics and biology. Funding for this award is provided by the Division of Physics and the Office of Multidisciplinary Activities in the Mathematical and Physical Sciences Directorate and by the Division of Molecular and Cellular Biosciences in the Biosciences Directorate.