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Localizing Chemical Groups while Imaging Single Native Proteins by High-Resolution Atomic Force Microscopy

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Department of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, 4058 Basel, Switzerland
§ Laboratory of Biomolecular Research, Department of Biology and Chemistry, Paul Scherrer Institut, 5232 Villingen, Switzerland
Cite this: Nano Lett. 2014, 14, 5, 2957–2964
Publication Date (Web):April 28, 2014
https://doi.org/10.1021/nl5012905
Copyright © 2014 American Chemical Society
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Abstract

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Simultaneous high-resolution imaging and localization of chemical interaction sites on single native proteins is a pertinent biophysical, biochemical, and nanotechnological challenge. Such structural mapping and characterization of binding sites is of importance in understanding how proteins interact with their environment and in manipulating such interactions in a plethora of biotechnological applications. Thus far, this challenge remains to be tackled. Here, we introduce force–distance curve-based atomic force microscopy (FD-based AFM) for the high-resolution imaging of SAS-6, a protein that self-assembles into cartwheel-like structures. Using functionalized AFM tips bearing Ni2+-N-nitrilotriacetate groups, we locate specific interaction sites on SAS-6 at nanometer resolution and quantify the binding strength of the Ni2+-NTA groups to histidine residues. The FD-based AFM approach can readily be applied to image any other native protein and to locate and structurally map histidine residues. Moreover, the surface chemistry used to functionalize the AFM tip can be modified to map other chemical interaction sites.

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Histograms of rupture forces and lengths detected between a Ni2+ NTA functionalized tip and Au surfaces derivatized with CGA-His6 peptides (Figure S1). Quality control of SAS-6 purity and of the specificity of the His6-tag engineered to SAS-6 (Figure S2). Histograms of rupture forces and lengths detected between a Ni2+ NTA functionalized tip and SAS-6 carrying a His6-tag (Figure S3). This material is available free of charge via the Internet at http://pubs.acs.org.

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