The Folding Type of a Protein Is Relevant to the Amino Acid Composition

抄録

The folding types of 135 proteins, the three-dimensional structures of which are known, were analyzed in terms of the amino acid composition. The amino acid composition of a protein was expressed as a point in a multidimensional space spanned with 20 axes, on which the corresponding contents of 20 amino acids in the protein were represented. The distribution pattern of proteins in this composition space was examined in relation to five folding types, α, β, α/β, α+β, and irregular type. The results show that amino acid compositions of the α, β, and α/β types are located in different regions in the composition space, thus allowing distinct separation of proteins depending on the folding types. The points representing proteins of the α+β and irregular types, however, are widely scattered in the space, and the existing regions overlap with those of the other folding types. A simple method of utilizing the “distance” in the space was found to be convenient for classification of proteins into the five folding types. The assignment of the folding type with this method gave an accuracy of 70% in the coincidence with the experimental data.