Sonja Müller-Späth

TL;DR: Forster resonance energy transfer was used in this article to investigate the influence of charged residues on the dimensions of unfolded and intrinsically disordered proteins, and it was shown that charge-balanced polypeptides can exhibit an additional collapse at low ionic strength, as predicted by polyampholyte theory.

TL;DR: The combination of single-molecule Förster resonance energy transfer, nanosecond fluorescence correlation spectroscopy, and microfluidic mixing is used to determine the reconfiguration times of unfolded proteins and investigate the mechanisms of internal friction contributing to their dynamics.

TL;DR: The results indicate an important role for additional temperature-dependent interactions within the unfolded chain in the extremely hydrophilic, intrinsically disordered protein prothymosin α.

TL;DR: This work uses single-molecule Forster resonance energy transfer to investigate the influence of charged residues on the dimensions of unfolded and intrinsically disordered proteins and finds that IDPs can exhibit a prominent expansion at low ionic strength that correlates with their net charge.

TL;DR: This chapter introduces the practical aspects of applying confocal single-molecule FRET experiments to the study of IDPs.