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.
component Protein Secondary Structure Physicochemical properties of amino acid Hydrophobicity
Gouchol Pok MingHao Piao Seung Jung Shin Keun Ho Ryu
Dept. of Computer Science Yanbian University of Science and Technology Yanji, China 133000 DB/Bioinformatics Lab Chungbuk National University, Cheongju, Korea 361-763 Division of Information Technology Hansei University, Gunpo Korea, 435-742
国际会议
上海
英文
148-151
2008-05-16(万方平台首次上网日期,不代表论文的发表时间)