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Structural Forces in Biomolecules

Published online by Cambridge University Press:  02 July 2020

Matthias Rief ,
Filipp Oesterhelt ,
Hauke Clausen-Schaumann  and
Hermann E. Gaub
Matthias Rief
Affiliation:
Department of Biochemistry, Stanford University School of Medicine
Filipp Oesterhelt
Affiliation:
Lehrstuhl f. angewandte Physik, Universität München
Hauke Clausen-Schaumann
Affiliation:
Lehrstuhl f. angewandte Physik, Universität München
Hermann E. Gaub
Affiliation:
Lehrstuhl f. angewandte Physik, Universität München
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Extract

The high spatial resolution and the force sensitivity of the Atomic Force Microscope have made it possible to perform mechanical experiments with single molecules. These experiments give direct access to the forces that stabilize biomolecule structure. In a variety of examples we show how different molecular interactions determine the mechanical stability of polysaccharides, proteins, DNA and other biomolecules.

Under the influence of a stretching force of around 750 pN the polysaccharide dextran undergoes a transition into a stretched conformation during which bond angles flip into a new conformation. Molecular dynamics simulations corroborated this conformational change.

Proteins fold into compact domains. Especially for structural proteins the mechanical stability of these domains is of importance. We show that the immunoglobulin and fibronectin III domains of the muscle protein titin exhibit exceptionally high unfolding forces (150-250 pN) when stretched at speeds of normal muscle operation (Fig. 1).

Type
Biological Applications of Scanning Probe Microscopies
Information
Microscopy and Microanalysis , Volume 5 , Issue S2: Proceedings: Microscopy & Microanalysis '99, Microscopy Society of America 57th Annual Meeting, Microbeam Analysis Society 33rd Annual Meeting, Portland, Oregon August 1-5, 1999 , August 1999 , pp. 1016 - 1017
Copyright
Copyright © Microscopy Society of America

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References

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