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. Author manuscript; available in PMC: 2011 Nov 14.
Published in final edited form as: Subcell Biochem. 2010;51:183–227. doi: 10.1007/978-90-481-8622-8_7

Fig. 7.1.

Fig. 7.1

A Distribution of amphipathic α-helices in the human exchangeable apolipoproteins, apoA-I and apoE. The letter P below the rectangles indicates positions of all proline residues. B Amphipathic helix classes found in the exchangeable apolipoproteins. Classification is based on the distribution of charged residues (see Section 2.1). These figures were adapted from Segrest et al. (1992)