Interrogating Single Molecules Using Force
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Dynamic single molecule force spectroscopy provides a powerful approach to probe the underlying energy landscape that governs how molecules fold, bind to each other, and undergo conformational transitions. These sophisticated experiments operate by imposing gradually increasing forces on single molecules and complexes and recording their force-extension behavior leading to eventual rupture. An outstanding question in this field is developing models to recover reliable estimates of the intrinsic energy landscape parameters from such force measurements. In this talk I will describe the development of new theoretical models for extracting the activation energy barriers and intrinsic transition rates from single-molecule force measurements [1,2]. The models go beyond the current state-of-the-art by accounting for both the finite stiffness of the pulling device and the non-linear stretching of the molecular handles connecting the molecule to the device. I will end the talk by discussing other biophysical problems currently being investigated in our laboratory, related to the in vivo structure, function, and regulation of DNA, chromatin, and chromosomes [3-6].