Speaker
Description
The TRPV1 ion channel is a heat sensor that plays a key role in pain sensing pathways. Recent advances in cryo-electron microscopy (cryo-EM) have facilitated a recent explosion in the availability of TRP channel structures. Despite these structures, the temperature-sensing mechanism of any TRP channel remains poorly understood. The manifold embedding method in cryo-EM allows the identification of free energy landscapes and related continuous molecular trajectories. Here, we apply this method to the original apo TRPV1 dataset at low temperature to find the conformations accessible via thermal motions, including the identification of motions of specific transmembrane helices. This result sets the stage for a better understanding of the TRPV1 temperature sensing mechanism via cryo-EM.
