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Figure 5 demonstrates the effect of temperature on movement between helices V and I in the correlation between cross-linking and transport activity, in which room temperature produced higher cross-linking in comparison to 0 degrees Celsius.

Figure 2 shows significant lactose transmembrane transport activity of double Cys mutants in RSO membrane vesicles

Figure 1A shows sugar-binding produces conformational change to open the periplasmic cavity resulting in the closing of cytoplasmic cavity

Figure 4 shows that helix VII opens on the periplasmic side for lactose transport in LacY. In the mutated single-Cys replacements, the helix VII showed increased reactivity towards the direction of the periplasmic side (direction of the black arrow) with sugar binding. Many of the single mutations had reactivity levels above the normalized level, representing increased reactivity. This demonstrates that helix VII is important for participating in the alternating access in the transportation of lactose.

Figure 6 demonstrates that there is an increase in accessibility/reactivity at the periplasmic end of helix VII on the periplasmic side of LacY during conformational changes