A theoretical method for distinguishing between soluble and membrane proteins.
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.
Yanagihara
N
N
Department of Material Systems Engineering, Faculty of Technology, Tokyo University of Agriculture and Technology, Japan.
Suwa
M
M
Mitaku
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002645:Chickens; D003574:Cytochrome c Group; D005583:Fourier Analysis; D006801:Humans; D008565:Membrane Proteins; D008722:Methods; D011487:Protein Conformation; D011506:Proteins; D012995:Solubility; D013816:Thermodynamics
D003574:Cytochrome c Group; D008565:Membrane Proteins; D011506:Proteins