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. Author manuscript; available in PMC: 2024 Apr 19.
Published in final edited form as: J Phys Chem Lett. 2016 Oct 26;7(21):4420–4426. doi: 10.1021/acs.jpclett.6b02159

Figure 5.

Figure 5.

Influence of bicelle size (q-factor) on protein-lipid contacts. Saturation transfers between protein backbone HN nuclei of (a) integrin αIIb and (b) β3(A711P) TM segments and either POPC(#3|CH2) or PC(#10|CH2) nuclei in q=0.5 and 0.7 bicelles. Tryptophan sidechain HN nuclei were also evaluated as shown using vertical labels. Black vertical lines indicate the previously determined membrane borders of αIIb and β3 TM helices.17,18 The POPC(#3|CH2)-HN transfer at the TM helix center of αIIb at q=0.7 is less efficient than at q=0.5 suggesting a heightened proportion of model II (Figure 2c) in q=0.7 bicelles.