Stepwise unfolding of titin under force-clamp atomic force microscopy |
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| Authors: | Oberhauser A F Hansma P K Carrion-Vazquez M Fernandez J M |
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| Affiliation: | Department of Physiology and Biophysics, Mayo Foundation, Rochester, MN 55905, USA. |
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| Abstract: | Here we demonstrate the implementation of a single-molecule force clamp adapted for use with an atomic force microscope. We show that under force-clamp conditions, an engineered titin protein elongates in steps because of the unfolding of its modules and that the waiting times to unfold are exponentially distributed. Force-clamp measurements directly measure the force dependence of the unfolding probability and readily captures the different mechanical stability of the I27 and I28 modules of human cardiac titin. Force-clamp spectroscopy promises to be a direct way to probe the mechanical stability of elastic proteins such as those found in muscle, the extracellular matrix, and cell adhesion. |
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