Fig. 3: hV1-S1S4 undergoes subtle temperature-induced changes in secondary structure.
From: Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
a Amide proton Δδ analysis identifies hV1-S1S4 secondary structure at elevated temperature (45 °C). b Dipolar wave analysis from RDC measurements of the hV1-S1S4 at 45 °C independently identifies secondary structure. c Amide proton Δδ analysis at 20 °C identifies that the hV1-S1S4 secondary structure is distinct from that at elevated temperature and generally consistent with cryo-EM secondary structures. In panels a–c, black circles are individual data points and are superimposed with fits of the data to an α-helical periodicity (red or blue lines respectively). d A bar plot of the amide proton temperature coefficients (ΔδHN/ΔT) against the hV1-S1S4 residue number. Values greater than −4.6 ppb K−1 are indicative of hydrogen bonding and are highlighted (blue). Light gray boxes indicate regions where NMR resonances are unassigned at 45 °C. ΔδHN/ΔT errors bars arise from fitting uncertainty. Source data are provided as a Source Data file.
