1989 年 29 巻 6 号 p. 284-289
The log P value used for the hydrophobicity parameter, where P is the partition coefficient in a 1-octanol/pH7.0 buffer system, of a number of di-pentapeptides was analyzed with physicochemical parameters for the side chain substituent of component amino acids. The log P value was shown to be governed not only by the "intrinsic" hydrophobicity but also by the steric effect of side chain substituents as well as intramolecular-type solvation and "polar proximity" effects for polar side chains. The β-turn conformational parameters of component amino acids devised from the Chou-Fasman propensity index was nicely applied for the analysis of log P value of tetra-and pentapeptides.