Markus Eilers

TL;DR: There is a strong linear correlation between the occurrence of residues in helix-helix interfaces and their packing values, and a second motif for mediating helix interactions is revealed by the high occurrence and high average packing values of small and polar residues in the helix interfaces of membrane proteins

TL;DR: NMR measurements reveal that structural changes in EL2 are coupled to the motion of helix H5 and breaking of the ionic lock that regulates activation in this prototypical G protein–coupled receptor.

TL;DR: Solid-state magic angle spinning NMR measurements are presented that support the proposal that interaction of Trp 265 with the retinal chromophore is responsible for stabilizing an inactive conformation in the dark, and that motion of the beta-ionone ring allows Trp265(6.48) and transmembrane helix H6 to adopt active conformations in the light.

TL;DR: Measurements of rhodopsin containing 13C-labeled histidine show that a strong hydrogen bond between the side-chain of Glu122 and the backbone carbonyl of His211 is disrupted in metarhodopin II, and the implications for the activation mechanism of r Rhodopsin are discussed.

TL;DR: The use of the helix packing moment is proposed as a complementary tool to the helical hydrophobic moment in the analysis of transmembrane sequences.