A theoretical method to characterize transmembrane helices by energy calculation was developed, in which interaction energy between a transmembrane helix and a probe helix was calculated. The applicability of this method was tested by using polyserine as a probe helix for the estimation of amphiphilicity of a given helix. The calculation for seven transmembrane helices of bacteriorhodopsin and halorhodopsin suggested that the angular profile of the interaction energy is closely related to the configuration of helices within the proteins and also to the two-dimensional crystalline array of bacteriorhodopsin.
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Suwa et al. (1992) studied this question.
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