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A group of exquisitely temperature-sensitive transient receptor potential channels,termed thermoTRPs, serve as cellular temperature sensors.How thermoTRPs can respond to temperature at different levels remains unknown.These channels are thought to adopt different conformations at varying temperatures, driven by a significant difference in free energy between the closed and open states.In support of this notion, we previously observed with site-directed fluorescence recordings that the pore region of TRPV1 channels undergoes substantial structural rearrangements during the heat activation.As structural knowledge of thermoTRPs is sparse, we modeled TRPV1 with Rosetta program in the closed state.To reveal structural changes that occur during heat activation, we are exploring the Rosetta modeling method to predict the structures of TRPV1 at different functional states.