Yanagihara N, Suwa M, Mitaku S
Department of Material Systems Engineering, Faculty of Technology, Tokyo University of Agriculture and Technology, Japan.
Biophys Chem. 1989 Sep 15;34(1):69-77. doi: 10.1016/0301-4622(89)80043-2.
A method for distinguishing between membrane and soluble proteins in an amino acid sequence was developed, using only two parameters associated with the hydrophobicity: the average hydrophobicity and the power spectral density of period longer than 30 residues. The power spectral density was calculated by a maximum entropy method of Fourier transformation. Membrane proteins could be distinguished from soluble proteins with a distinction rate as high as 97%. This fact strongly suggests that the morphology of proteins, i.e., membrane or soluble forms, is determined thermodynamically through the hydrophobicity of polypeptides.
