Proteins are not always rigid structures. Many of their most important parts — linkers, loops, and disordered regions — are highly flexible, constantly changing shape in solution. To understand how these regions behave, scientists often study short model peptides that capture the essential physics of flexibility.

In a new article [1], I have explored the behavior of glycine- and serine-rich octapeptides using molecular dynamics simulations combined with concepts from FRET (Förster Resonance Energy Transfer) spectroscopy.