Fig. 4: hV1-S1S4 undergoes discrete temperature-induced changes in distances, and solvent accessibility.
From: Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing

a Temperature-dependent differences in distances measured using paramagnetic relaxation enhancement (ΔPRE) of the hV1-S1S4 at 20 and 50 °C. The average of the s.e.m, 1.2 Å, was used as a threshold value and shown in gray. Errors are propagated s.e.m. b Changes in hydration as a function of temperature were measured from normalized HN–water resonance intensities from 15N-NOESY-TROSY data at 20 and 45 °C. The ΔNOE45 °C−20 °C is reflective of changes in hydration where loops and the bottom of S4 helix exhibit increased hydration at elevated temperatures. c A cartoon of hV1-S1S4 identifying regions that change as a function of temperature. Blue and magenta circles indicate increased and decreased helicity, respectively. The green circle highlights differences in the S1–S2 loop solvent accessibility. Transmembrane helix distortions are highlighted as transparent cyan circles. The blue highlighted region shows helical differences in the vanilloid binding site and the magenta identifies the C-terminus of the S4 helix which becomes more solvent exposed and less helical at elevated temperatures. Source data are provided as a Source Data file.