In Science this week, a multi-institute team of investigators reports new details about the molecular chaperone Trigger Factor, which prevents the aggregation and misfolding of proteins. Using nuclear magnetic resonance and isotope labeling techniques, they show the structure and dynamics of three Trigger Factor molecules in complex with an unfolded alkaline phosphatase substrate. They also demonstrate how Trigger Factor, which does not require ATP to bind to substrates, uses four flexible, hydrophobic binding sites on its inner surface to interact with a wide range of peptide stretches. Further, they state that many Trigger Factor molecules can bind to a substrate simultaneously and the Trigger Factor/substrate complex appears to get more stable as more stretches of alkaline phosphatase are added to it.