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Utilizing Single-Molecule Fret Methods To Study Conformational Changes In Trim5Α, Margret Suzanne Bradley
Utilizing Single-Molecule Fret Methods To Study Conformational Changes In Trim5Α, Margret Suzanne Bradley
Master's Theses
Single-molecule FRET (smFRET) is a method by which dynamic conformational changes can be monitored in a protein microscopically and in real time. smFRET relies on the creation of FRET (Förster Resonance Energy Transfer) between small molecule fluorophores conjugated to the biomolecules of interest. FRET efficiency allows calculation of interfluorophore distances. Changes in FRET efficiency represent changes in protein conformation which can inform further structural and molecular studies of the protein of interest. For example, in the Campbell Lab, we study the protein TRIM5α, an antiretroviral cellular protein which can cause premature dissociation of the HIV capsid core by an unknown …