Temperature-controlled nanoaperture optical trapping

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dc.contributor.authorLetwin, Keiran
dc.contributor.supervisorGordon, Reuven
dc.date.accessioned2025-10-01T20:45:13Z
dc.date.available2025-10-01T20:45:13Z
dc.date.issued2025
dc.degree.departmentDepartment of Electrical and Computer Engineering
dc.degree.levelMaster of Applied Science MASc
dc.description.abstractNanoaperture optical trapping (NOT) enables the capture of single proteins to detect their conformational dynamics without labeling or tethering, thus preserving their structure. Protein folding is highly sensitive to environmental conditions, making the investigation of thermodynamic parameters a robust method for probing conformational stability. While previous studies have employed laser-induced heating to modulate the local temperature, such methods are limited in accessing broader temperature ranges. In this work, the low-temperature dynamics of individual Bovine Serum Albumin (BSA) are investigated using a custom-built temperature-controlled stage. The transitions between the normal (N) and fast (F) conformational states of BSA were uncovered. Notably, the N form exhibited a maximum occupancy at \(21 \pm 1\,^{\circ}\mathrm{C}\), which was interpreted as the point of maximal thermodynamic stability for the compact N state relative to the F state. This approach enabled the extraction of single-molecule thermodynamic parameters without requiring modification to the protein's native structure, providing a multifaceted NOT method for broad applications.
dc.description.scholarlevelGraduate
dc.identifier.urihttps://hdl.handle.net/1828/22825
dc.languageEnglisheng
dc.language.isoen
dc.rightsAvailable to the World Wide Web
dc.subjectNanoaperture optical trapping
dc.subjectProtein conformational dynamics
dc.subjectLabel-free
dc.subjectThermodynamic
dc.subjectTemperature-controlled
dc.titleTemperature-controlled nanoaperture optical trapping
dc.typeThesis

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