Probing both sides of the story

doi:10.1073/pnas.2212419119

. 2022 Sep 20;119(38):e2212419119.

doi: 10.1073/pnas.2212419119. Epub 2022 Sep 7.

Probing both sides of the story

Christopher M Yip^{1

2

3

4}

Affiliations

¹ Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E9, Canada.
² Institute of Biomedical Engineering, University of Toronto, Toronto, ON M5S 3E9, Canada.
³ Department of Biochemistry, University of Toronto, Toronto, ON M5S 3E9, Canada.
⁴ Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON M5S 3E9, Canada.

PMID: 36070345
PMCID: PMC9499575
DOI: 10.1073/pnas.2212419119

Probing both sides of the story

Christopher M Yip. Proc Natl Acad Sci U S A. 2022.

. 2022 Sep 20;119(38):e2212419119.

doi: 10.1073/pnas.2212419119. Epub 2022 Sep 7.

Author

Christopher M Yip^{1

2

3

4}

Affiliations

¹ Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E9, Canada.
² Institute of Biomedical Engineering, University of Toronto, Toronto, ON M5S 3E9, Canada.
³ Department of Biochemistry, University of Toronto, Toronto, ON M5S 3E9, Canada.
⁴ Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON M5S 3E9, Canada.

PMID: 36070345
PMCID: PMC9499575
DOI: 10.1073/pnas.2212419119

No abstract available

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Conflict of interest statement

The author declares no competing interest.

Figures

**Fig. 1.**
Schematic representation of two tip-enhanced nanospectroscopy platforms. (A) TIR-s-SNOM with the AFM tip positioned to scan the surface of an ATR prism, enabling simultaneous image and spectral acquisition; (B) nano-FTIR/s-SNOM configuration using a graphene membrane as a substrate, with the FTIR and AFM datasets collected separately.

See this image and copyright information in PMC

Comment on

doi: 10.1073/pnas.2200019119

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References

1. Zhao X., Li D., Lu Y.-H., Salmeron M. B., In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale. Proc. Natl. Acad. Sci. U.S.A. 119, 10.1073/pnas.2200019119 (2022). - DOI - PMC - PubMed
1. Jiao F., Cannon K. S., Lin Y. C., Gladfelter A. S., Scheuring S., The hierarchical assembly of septins revealed by high-speed AFM. Nat. Commun. 11, 5062 (2020). - PMC - PubMed
1. Sanganna Gari R. R., et al. , Correlation of membrane protein conformational and functional dynamics. Nat. Commun. 12, 4363 (2021). - PMC - PubMed
1. Umakoshi T., Fukuda S., Iino R., Uchihashi T., Ando T., High-speed near-field fluorescence microscopy combined with high-speed atomic force microscopy for biological studies. Biochim. Biophys. Acta Gen. Subj. 1864, 129325 (2020). - PubMed
1. De Keersmaecker H., et al. , Correlative atomic force and single-molecule fluorescence microscopy of nucleoprotein complexes. Methods Mol. Biol. 1814, 339–359 (2018). - PubMed

Grants and funding

RGPIN-2022-048/Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (NSERC)

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[1] Zhao X., Li D., Lu Y.-H., Salmeron M. B., In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale. Proc. Natl. Acad. Sci. U.S.A. 119, 10.1073/pnas.2200019119 (2022). - DOI - PMC - PubMed

[2] Zhao X., Li D., Lu Y.-H., Salmeron M. B., In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale. Proc. Natl. Acad. Sci. U.S.A. 119, 10.1073/pnas.2200019119 (2022). - DOI - PMC - PubMed

[3] Jiao F., Cannon K. S., Lin Y. C., Gladfelter A. S., Scheuring S., The hierarchical assembly of septins revealed by high-speed AFM. Nat. Commun. 11, 5062 (2020). - PMC - PubMed

[4] Jiao F., Cannon K. S., Lin Y. C., Gladfelter A. S., Scheuring S., The hierarchical assembly of septins revealed by high-speed AFM. Nat. Commun. 11, 5062 (2020). - PMC - PubMed

[5] Sanganna Gari R. R., et al. , Correlation of membrane protein conformational and functional dynamics. Nat. Commun. 12, 4363 (2021). - PMC - PubMed

[6] Sanganna Gari R. R., et al. , Correlation of membrane protein conformational and functional dynamics. Nat. Commun. 12, 4363 (2021). - PMC - PubMed

[7] Umakoshi T., Fukuda S., Iino R., Uchihashi T., Ando T., High-speed near-field fluorescence microscopy combined with high-speed atomic force microscopy for biological studies. Biochim. Biophys. Acta Gen. Subj. 1864, 129325 (2020). - PubMed

[8] Umakoshi T., Fukuda S., Iino R., Uchihashi T., Ando T., High-speed near-field fluorescence microscopy combined with high-speed atomic force microscopy for biological studies. Biochim. Biophys. Acta Gen. Subj. 1864, 129325 (2020). - PubMed

[9] De Keersmaecker H., et al. , Correlative atomic force and single-molecule fluorescence microscopy of nucleoprotein complexes. Methods Mol. Biol. 1814, 339–359 (2018). - PubMed

[10] De Keersmaecker H., et al. , Correlative atomic force and single-molecule fluorescence microscopy of nucleoprotein complexes. Methods Mol. Biol. 1814, 339–359 (2018). - PubMed

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Probing both sides of the story

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Probing both sides of the story

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Conflict of interest statement

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