Work

Stepwise unfolding of titin under force-clamp atomic force microscopy

Year: 2001

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.98.2.468

Authors: Andres F. Oberhauser, Paul K. Hansma, Mariano Carrion-Vazquez, Julio M. Fernandez

Institution: University of California, Santa Barbara

Language: English

Topic: Force Microscopy Techniques and Applications

Subfield: Atomic and Molecular Physics, and Optics

Field: Physics and Astronomy

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Heart, Lung, and Blood Institute

Awards: Nanomechanics of the extracellular matrix, Single molecule studies of titin elasticity