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Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...
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Updated: Mar 27, 2026

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Structural energetics of cold sensitivity.

Kevin Y Choi1,2,3, Xiaoxuan Lin4, Yifan Cheng5,6

  • 1Department of Biochemistry and Biophysics, University of California San Franscisco, San Francisco, CA, USA.

Nature
|March 26, 2026
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Summary
This summary is machine-generated.

Researchers uncovered the structural mechanism behind cold sensation, revealing how the TRPM8 (transient receptor potential melastatin 8) channel opens in response to cold temperatures. This finding clarifies how we perceive cold and use of cooling agents.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Thermosensitive transient receptor potential (TRP) ion channels are crucial for detecting thermal changes in the environment.
  • The menthol receptor, TRPM8, is activated by temperatures below 26°C and mediates cold perception.
  • Understanding the structural and thermodynamic mechanisms of thermosensitive channel gating remains a significant challenge.

Purpose of the Study:

  • To elucidate the mechanism of cold-evoked activation of the TRPM8 channel.
  • To visualize temperature-evoked conformational states and assess the energetic landscape of gating transitions.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to visualize TRPM8 channel structures.
  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS) was employed to identify regions with stimulus-evoked energetic changes.
  • Structural mechanisms were validated by comparing human TRPM8 with its avian orthologue.

Main Results:

  • Cryo-EM captured bona fide menthol- and cold-evoked open states of TRPM8.
  • A novel 'semi-swapped' architecture was identified, involving rearrangement of channel subunits and repositioning of the S6 helix.
  • HDX-MS pinpointed the pore and TRP helices as key regions driving gating through stimulus-evoked energetic changes.
  • Cold-evoked stabilization of the outer pore region was shown to reposition the S6 helix and facilitate regulatory lipid binding, stabilizing the open channel.

Conclusions:

  • A detailed structural and thermodynamic mechanism for cold-evoked TRPM8 activation has been elucidated.
  • The findings provide insights into the gating mechanism of thermosensitive ion channels.
  • The study proposes a free energy landscape and conformational pathway for TRPM8 activation by cold or cooling agents.