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. 2015 Feb 3;7(2):407–422. doi: 10.3390/toxins7020407

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Aromatic amino acid residues of HALT-1, EqtII and StnII. All residues are shown as sticks in different colours. (A) Tyr110 (skyblue), Trp113 (magenta) and Tyr129 (yellow) from HALT-1; (B) Tyr113, (skyblue), Trp116 (magenta) and Tyr137 (yellow) from EqtII; (C) Tyr111 (skyblue), Trp114 (magenta) and Trp135 (yellow) from StnII. All these tyrosine (Tyr) and tryptophan (Trp) are well conserved between HALT-1, EqtII and StnII and they are predicted to form an aromatic patch on surface of the molecule which could be essential for the insertion into water-lipid interface.

Aromatic amino acid residues of HALT-1, EqtII and StnII. All residues are shown as sticks in different colours. (A) Tyr110 (skyblue), Trp113 (magenta) and Tyr129 (yellow) from HALT-1; (B) Tyr113, (skyblue), Trp116 (magenta) and Tyr137 (yellow) from EqtII; (C) Tyr111 (skyblue), Trp114 (magenta) and Trp135 (yellow) from StnII. All these tyrosine (Tyr) and tryptophan (Trp) are well conserved between HALT-1, EqtII and StnII and they are predicted to form an aromatic patch on surface of the molecule which could be essential for the insertion into water-lipid interface.