Landing proteins on graphene trampoline preserves their gas-phase folding on the surface
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 tha...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
American Chemical Society
2022
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| _version_ | 1797109528068620288 |
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| author | Anggara, K Ochner, H Szilagyi, S Malavolti, L Rauschenbach, S Kern, K |
| author_facet | Anggara, K Ochner, H Szilagyi, S Malavolti, L Rauschenbach, S Kern, K |
| author_sort | Anggara, K |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T07:43:00Z |
| format | Journal article |
| id | oxford-uuid:c70645d4-ebe9-4bc7-a92e-310ea89e678d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T07:43:00Z |
| publishDate | 2022 |
| publisher | American Chemical Society |
| record_format | dspace |
| spelling | oxford-uuid:c70645d4-ebe9-4bc7-a92e-310ea89e678d2023-05-12T06:36:59ZLanding proteins on graphene trampoline preserves their gas-phase folding on the surfaceJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c70645d4-ebe9-4bc7-a92e-310ea89e678dEnglishSymplectic ElementsAmerican Chemical Society2022Anggara, KOchner, HSzilagyi, SMalavolti, LRauschenbach, SKern, KMolecule-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. |
| spellingShingle | Anggara, K Ochner, H Szilagyi, S Malavolti, L Rauschenbach, S Kern, K 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 |
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