Conformational stability at low temperatures using single protein nanoaperture optical tweezers

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dc.contributor.authorLetwin, Keiran
dc.contributor.authorPeters, Matthew
dc.contributor.authorGordon, Reuven
dc.date.accessioned2025-03-20T16:08:05Z
dc.date.available2025-03-20T16:08:05Z
dc.date.issued2025
dc.description.abstractNanoaperture optical tweezers allow for trapping single proteins and detecting their conformational changes without modifying the protein, i.e., being free from labels or tethers. While past works have used laser heating as a way to vary the local temperature, this does not allow for probing of lower temperature values. Here we investigate the lower temperature dynamics of individual Bovine Serum Albumin (BSA) proteins with the help of a custom Peltier cooling stage. The BSA transitions between the normal (N) and fast (F) states. The normal form of BSA has a maximum occupancy at 21 ± 1 °C, which is interpreted as its maximum stability point for the compact N form with respect to the F form. In this way, it is possible to find the relative thermodynamic parameters of single proteins without requiring any modifications to the intrinsic structure.
dc.description.reviewstatusReviewed
dc.description.scholarlevelFaculty
dc.description.sponsorshipThe authors acknowledge support from NSERC Discovery Grant RGPIN-2023-04-18.
dc.identifier.citationLetwin, K., Peters, M., & Gordon, R. (2025). Conformational stability at low temperatures using single protein nanoaperture optical tweezers. The Journal of Physical Chemistry B, 129(9), 2402–2407. https://doi.org/10.1021/acs.jpcb.4c07987
dc.identifier.urihttps://doi.org/10.1021/acs.jpcb.4c07987
dc.identifier.urihttps://hdl.handle.net/1828/21676
dc.language.isoen
dc.publisherThe Journal of Physical Chemistry B
dc.subjectethanol
dc.subjectfree energy
dc.subjectlasers
dc.subjectpower
dc.subjectstability
dc.titleConformational stability at low temperatures using single protein nanoaperture optical tweezers
dc.typePostprint

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