Abstract
One of the goals of the Petersson laboratory is to develop new methods to study the misfolding of amyloidogenic proteins. Due to their inherent structural heterogeneity, these proteins can be difficult to characterize by traditional structural methods (e.g. crystallography). Fluorescence spectroscopy provides a powerful tool to study protein folding and misfolding in real-time, but its employment requires labeling the protein of interest with two or more fluorophores. We have developed methods to combine multiple orthogonal labeling techniques to produce homogenous double-labeled α-synuclein for Forster resonance energy transfer (FRET) studies. Ultimately, these studies will aid in understanding protein misfolding implicated in neurodegenerative disease.
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