Abstract
Within the arsenal of experimental methods in studying intrinsically disordered proteins (IDPs), single-molecule fluorescence methods provide unique long-range distance and dynamics information. In this chapter, we discuss recent progress on using single-molecule fluorescence methods for probing both intra- and intermolecular interactions of IDPs. We focus on several aspects, including models for analyzing experimental data, physical principles that can be obtained, and combinations with other experimental methods for a comprehensive view of the structural properties of IDPs.
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