In
this thesis single-molecule fluorescence resonance energy transfer
(FRET)
spectroscopy was used to study the folding of a protein that belongs
to the large and important family of repeat proteins. Cohen shows
that the dynamics of the expanded conformations is likely to be very
fast, suggesting a spring-like motion of the whole chain. The
findings shed new light
on the elasticity of structure in repeat proteins, which is related
to their function in binding multiple and disparate partners. This
concise research summary provides useful insights for students
beginning a PhD in this or a related area, and researchers entering
this field.