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Mechanical Mapping of Single Membrane Proteins at Submolecular Resolution

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Institut Curie, U1006 INSERM, 26 rue d’Ulm, 75005 Paris, France
Bruker Nano, Inc., 112 Robin Hill Road, Santa Barbara, California 93117, United States
Tel: +33 1 56 24 67 81. Fax: +33 1 40 51 06 36. E-mail: [email protected]
Cite this: Nano Lett. 2011, 11, 9, 3983–3986
Publication Date (Web):August 1, 2011
https://doi.org/10.1021/nl202351t
Copyright © 2011 American Chemical Society
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Abstract

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The capacity of proteins to carry out different functions is related to their ability to undergo conformation changes, which depends on the flexibility of protein structures. In this work, we applied a novel imaging mode based on indentation force spectroscopy to map quantitatively the flexibility of individual membrane proteins in their native, folded state at unprecedented submolecular resolution. Our results enabled us to correlate protein flexibility with crystal structure and showed that α-helices are stiff structures that may contribute importantly to the mechanical stability of membrane proteins, while interhelical loops appeared more flexible, allowing conformational changes related to function.

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