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Landing Proteins on Graphene Trampoline Preserves Their Gas-Phase Folding on the Surface
[Image: see text] Molecule–surface collisions are known to initiate dynamics that lead to products inaccessible by thermal chemistry. These collision dynamics, however, have mostly been examined on bulk surfaces, leaving vast opportunities unexplored for molecular collisions on nanostructures, espec...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951278/ https://www.ncbi.nlm.nih.gov/pubmed/36844500 http://dx.doi.org/10.1021/acscentsci.2c00815 |
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author | Anggara, Kelvin Ochner, Hannah Szilagyi, Sven Malavolti, Luigi Rauschenbach, Stephan Kern, Klaus |
author_facet | Anggara, Kelvin Ochner, Hannah Szilagyi, Sven Malavolti, Luigi Rauschenbach, Stephan Kern, Klaus |
author_sort | Anggara, Kelvin |
collection | PubMed |
description | [Image: see text] Molecule–surface collisions are known to initiate dynamics that lead to products inaccessible by thermal chemistry. These collision dynamics, however, have mostly been examined on bulk surfaces, leaving vast opportunities unexplored for molecular collisions on nanostructures, especially on those that exhibit mechanical properties radically different from those of their bulk counterparts. Probing energy-dependent dynamics on nanostructures, particularly for large molecules, has been challenging due to their fast time scales and high structural complexity. Here, by examining the dynamics of a protein impinging on a freestanding, single-atom-thick membrane, we discover molecule-on-trampoline dynamics that disperse the collision impact away from the incident protein within a few picoseconds. As a result, our experiments and ab initio calculations show that cytochrome c retains its gas-phase folded structure when it collides onto freestanding single-layer graphene at low energies (∼20 meV/atom). The molecule-on-trampoline dynamics, expected to be operative on many freestanding atomic membranes, enable reliable means to transfer gas-phase macromolecular structures onto freestanding surfaces for their single-molecule imaging, complementing many bioanalytical techniques. |
format | Online Article Text |
id | pubmed-9951278 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-99512782023-02-25 Landing Proteins on Graphene Trampoline Preserves Their Gas-Phase Folding on the Surface Anggara, Kelvin Ochner, Hannah Szilagyi, Sven Malavolti, Luigi Rauschenbach, Stephan Kern, Klaus ACS Cent Sci [Image: see text] Molecule–surface collisions are known to initiate dynamics that lead to products inaccessible by thermal chemistry. These collision dynamics, however, have mostly been examined on bulk surfaces, leaving vast opportunities unexplored for molecular collisions on nanostructures, especially on those that exhibit mechanical properties radically different from those of their bulk counterparts. Probing energy-dependent dynamics on nanostructures, particularly for large molecules, has been challenging due to their fast time scales and high structural complexity. Here, by examining the dynamics of a protein impinging on a freestanding, single-atom-thick membrane, we discover molecule-on-trampoline dynamics that disperse the collision impact away from the incident protein within a few picoseconds. As a result, our experiments and ab initio calculations show that cytochrome c retains its gas-phase folded structure when it collides onto freestanding single-layer graphene at low energies (∼20 meV/atom). The molecule-on-trampoline dynamics, expected to be operative on many freestanding atomic membranes, enable reliable means to transfer gas-phase macromolecular structures onto freestanding surfaces for their single-molecule imaging, complementing many bioanalytical techniques. American Chemical Society 2022-12-14 /pmc/articles/PMC9951278/ /pubmed/36844500 http://dx.doi.org/10.1021/acscentsci.2c00815 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Anggara, Kelvin Ochner, Hannah Szilagyi, Sven Malavolti, Luigi Rauschenbach, Stephan Kern, Klaus Landing Proteins on Graphene Trampoline Preserves Their Gas-Phase Folding on the Surface |
title | Landing Proteins on Graphene Trampoline Preserves
Their Gas-Phase Folding on the Surface |
title_full | Landing Proteins on Graphene Trampoline Preserves
Their Gas-Phase Folding on the Surface |
title_fullStr | Landing Proteins on Graphene Trampoline Preserves
Their Gas-Phase Folding on the Surface |
title_full_unstemmed | Landing Proteins on Graphene Trampoline Preserves
Their Gas-Phase Folding on the Surface |
title_short | Landing Proteins on Graphene Trampoline Preserves
Their Gas-Phase Folding on the Surface |
title_sort | landing proteins on graphene trampoline preserves
their gas-phase folding on the surface |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951278/ https://www.ncbi.nlm.nih.gov/pubmed/36844500 http://dx.doi.org/10.1021/acscentsci.2c00815 |
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