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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2010 Aug 16;1808(1):34–40. doi: 10.1016/j.bbamem.2010.08.008

Figure 1.

Figure 1

(A) Amino acid sequence of distinctin heterodimer. 15N labeled amino acids are highlighted in blue. Residue Cys-19 of chain 1 and Cys-23 of chain 2 are involved in a disulfide bridge. (B) Helical wheel plots showing the amphipathic nature of each chain. Hydrophobic residues are in red. (C) Three-dimensional structure of distinctin in aqueous buffer [29]. The four-helical bundle is stabilized by hydrophobic interactions of the residues, forming a hydrophobic core in the interior of the structure.