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Stretching single molecules into novel conformations using the atomic force microscope

Abstract

A dense network of interconnected proteins and carbohydrates forms the complex mechanical scaffold of living tissues. The recently developed technique of single molecule force spectroscopy using the atomic force microscope (AFM) has enabled a detailed analysis of the force-induced conformations of these molecules and the determinants of their mechanical stability. These studies provide some of the basic knowledge required to understand the mechanical interactions that define all biological organisms.

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Figure 1: The extension of modular proteins with the AFM.
Figure 2: Identification of an unfolding intermediate in the extension of I27 and the prevention of this intermediate by a point mutation.
Figure 3: The engineering of polyproteins to probe the structure of immunoglobulin domains.

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Acknowledgements

We thank A. Oberhauser, M. Carrion-Vazquez and H. Li for ideas, data and figures for this review and K. Schulten for the images in Fig. 2b.

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Correspondence to Julio M. Fernandez.

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Fisher, T., Marszalek, P. & Fernandez, J. Stretching single molecules into novel conformations using the atomic force microscope. Nat Struct Mol Biol 7, 719–724 (2000). https://doi.org/10.1038/78936

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