Extended Data Figure 3: Positions of transmembrane helices.
From: Architecture and conformational switch mechanism of the ryanodine receptor
a, The probability for the formation of transmembrane helices calculated by the program TMHMM is shown for the C-terminal region of RyR1. Red bars indicate α-helices predicted in SABLE. The consensus transmembrane (TM) helices are unambiguously recognized and clearly separated, except of TM3 and TM4, which have nearly no solvent exposed loop in between. The amphipathic and pore helices are also clearly indicated, but have lower hydrophobicity scores than the transmembrane helices. b, Experimental mapping and prediction of transmembrane helices. Sequence ranges of computationally predicted, annotated and experimentally mapped transmembrane helices. Consensus helices between experimental mapping and computational prediction are indicated in bold. Although computational methods suggest just one TM3 helix instead of TM3/4, the width of the hydrophobic region corresponding to helix TM3 is consistent with the presence of two joint transmembrane helices as observed in the topology mapping experiments14.
