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Mapping Single-molecule Protein Complexes in 3D with DNA Nanoswitch Calipers
Open accessPreprint — published as 10.1021/jacs.3c10262
Abstract
The ability to accurately map the 3D geometry of single-molecule complexes in trace samples 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, which we have previously introduced, 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 to previously reported structures.
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Metadata
- Authors
- Shrestha, P., Yang, D., Shih, W. M., & Wong, W. P.
- Affiliations
- Boston Children's Hospital (US)
- Harvard University (US)
- Corresponding author
- Wong, Wesley P.
- Venue
- Journal of the American Chemical Society
- Publisher
- openRxiv
- Published
- 2023-07-11
- Volume
- 145
- Issue
- 51
- Pages
- 27916-27921
- ISSN
- 0002-7863 (ISSN-L)
- PMC
- PMC10755700
- OpenAlex
- W4389764840
- Cited by
- 5
- References
- 1
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Journal of the American Chemical Society (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Alfred P. Sloan Foundation (G-2021-169145)
- Harvard University
- National Institutes of Health
- Hansjörg Wyss Institute for Biologically Inspired Engineering, Harvard University
- Office of Naval Research (N00014-15-1-0073)
- National Institute of General Medical Sciences (GM119537, R35GM119537)
- Topics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced biosensing and bioanalysis techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Keywords
- single-molecule force spectroscopy, streptavidin, biotin binding site, tetrahedral geometry, nanodevices
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