Fig. 4: Hydrophobicity in the H2 region drives membrane interaction of the NHE1-LID. | Communications Biology

Fig. 4: Hydrophobicity in the H2 region drives membrane interaction of the NHE1-LID.

From: The intracellular lipid-binding domain of human Na+/H+ exchanger 1 forms a lipid-protein co-structure essential for activity

Fig. 4

a Three different variants of the NHE1-LID539-593 were analyzed, NHE1-LID539-593-2G-1 (I574G, F576G in HM1), NHE1-LID539-593-2G-2 (I586G, L588G in HM2) and NHE1-LID539-593-4G (I574G, F576G, I586G, L588G), as indicated. b Far-UV CD spectra of cLID567-592 peptides with glycine mutations in various lipids. c Far UV CD spectra of NHE1-LID LID539-593-4G alone (black) and in the presence of 2% LPPG (color) and DMPG:DMPC:DHPC bicelles (dashed color). d 15N,1H-HSQC spectrum of NHE1-LID LID539-593-4G in H2O, pH 6.5. e Differences in SCS between NHE1-LID539-593 and NHE1-LID539-593-4G in the absence of membrane mimetics. Top: ΔSCSs of Cα, bottom: Differences in amide shifts given by ΔδNHs.

Back to article page