Mapping Single-Molecule Protein Complexes in 3D with DNA Nanoswitch Calipers
The ability to accurately map the 3D geometry of single-molecule complexes in trace samples is a challenging goal that would lead to new insights into molecular mechanics and provide an approach for single-molecule structural proteomics. To enable this, we have developed a high-resolution force spectroscopy method capable of measuring multiple distances between labeled sites in natively folded protein complexes. Our approach combines reconfigurable nanoscale devices, we call DNA nanoswitch calipers, with a force-based barcoding system to distinguish each measurement location. We demonstrate our approach by reconstructing the tetrahedral geometry of biotin-binding sites in natively folded streptavidin, with 1.5-2.5 Å agreement with previously reported structures.
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| Medienart: |
E-Artikel |
| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:145 |
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| Enthalten in: |
Journal of the American Chemical Society - 145(2023), 51 vom: 27. Dez., Seite 27916-27921 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Shrestha, Prakash [VerfasserIn] |
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| Links: |
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| Themen: |
6SO6U10H04 |
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| Anmerkungen: |
Date Completed 28.12.2023 Date Revised 14.02.2024 published: Print-Electronic UpdateOf: bioRxiv. 2023 Jul 11;:. - PMID 37502860 Citation Status MEDLINE |
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| doi: |
10.1021/jacs.3c10262 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a The ability to accurately map the 3D geometry of single-molecule complexes in trace samples is a challenging goal that would lead to new insights into molecular mechanics and provide an approach for single-molecule structural proteomics. To enable this, we have developed a high-resolution force spectroscopy method capable of measuring multiple distances between labeled sites in natively folded protein complexes. Our approach combines reconfigurable nanoscale devices, we call DNA nanoswitch calipers, with a force-based barcoding system to distinguish each measurement location. We demonstrate our approach by reconstructing the tetrahedral geometry of biotin-binding sites in natively folded streptavidin, with 1.5-2.5 Å agreement with previously reported structures | ||
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| 700 | 1 | |a Shih, William M |e verfasserin |4 aut | |
| 700 | 1 | |a Wong, Wesley P |e verfasserin |4 aut | |
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