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. 2019 Sep 24;6:83. doi: 10.3389/fmolb.2019.00083

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Copyright © 2019 Salnikov, Aisenbrey, Pokrandt, Brügger and Bechinger.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Analysis of NMR topological restraints for a DQB1 ideal helix reconstituted into mechanically oriented DMPC (A,C,E) or POPC/SM (95/5) membranes at 1 mole% (B,D,F). The topological restraints from each NMR measurement are shown for ¹⁵N-V14 in red (208 ± 3.5 ppm for DMPC and 213 ± 4 ppm for POPC/SM), and for ¹⁵N-L15 in blue (191.5 ± 4 ppm for DMPC and 196 ± 6 ppm for POPC/SM). The restraints were obtained assuming either a static peptide alignment (A,B) or rocking and wobbling motions of the helix resulting in a Gaussian distribution of SD 12° and 40°, respectively (C,D) or of 12° and 80°, respectively (E,F). The central line represents the main intensity, two additional restrictions were calculated from the ¹⁵N chemical shifts defining the LWHH to take into account orientational distributions and potential errors.