Fig. 2: Helix stabilities and conformational plasticity at 310 K.
From: Thermodynamic architecture and conformational plasticity of GPCRs
a Box plot of individual TM helix stabilities (n = 45). Box plots include the median line (median value indicated), the box denotes the interquartile range (IQR), whiskers denote the rest of the data distribution, and outliers are denoted by points greater than ±1.5 × IQR. b One-dimensional free energy profiles of two representative GPCRs. The vertical dashed lines signal the reaction coordinate (RC) values of 0.85 (continuous red) and 0.7 (dashed red), respectively. c, d Protein regions that unfold first as one moves from the right to the left on the free energy profiles are illustrated by dividing the GPCR structures into the N-terminal half (TM helices 1–3) and C-terminal half (TM helices 4–7). c, d plot the means folding probability of the N- and C-terminal halves of the structure at the indicated reaction coordinate values. Source data are provided as a Source data file.
