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Intriguingly, “the periplasmic domains of NccX appeared collapsed against the hydrophobic TM segments, leading to an aberrant topology incompatible with membrane insertion.” The authors explained this unusual topology with a “detergent-induced redistribution of the hydrophobic interactions among the TM helices and a pair of hydrophobic patches keeping the periplasmic domains together in the native dimer.” In this case, alkyl phosphocholine led to a very unusual architecture that does not seem to be of biological relevance

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Final Thoughts: Is DSIP the Next Frontier in Sleep Medicine Research