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Figure 10 | BMC Structural Biology

Figure 10

From: Progesterone modulation of transmembrane helix-helix interactions between the α-subunit of Na/K-ATPase and phospholipid N-methyltransferase in the oocyte plasma membrane

Figure 10

Helical wheel representations of the amino acid sequences of the M2 helix of the α1-subunit of the Na, K-ATPase and helix M3 of the PE NMT. The amino acid side chains are projected down the axis of the alpha helix (orthogonal to the plane of the page). The nonpolar residues are in yellow, the polar, uncharged residues are green. As an ideal alpha helix consists of 3.6 residues per complete turn, the angle between two residues is chosen to be 100 degrees and thus there exists a periodicity after five turns and 18 residues. The Figure is a snapshot of a Java Applet written by Edward K. O'Neil and Charles M. Grisham, University of Virginia at Charlottsville, VA (see Methods).

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