Hydrophobic Amino Acid Composition Patterns over Secondary Structure Elements of Proteins

As evidenced by a buried core of hydrophobic residues within globular proteins, hydrophobicity provides essential insights into the folding structure of proteins. Previous studies have shown that hydrophobic residues show statistically meaningful distribution on the primary sequence, but most of them lacked further investigation into a potential relationship to secondary structure elements. In this paper we experimentally show that the hydrophobic residues collectively reveal different composition patterns over different secondary structure elements. After visually presenting the class-specific features, we quantitatively compare them using the statistical moments.