Protein binding predictions from amino acid primary sequence hydrophobicity

✍ Scribed by Arnold J. Mandell; Karen A. Selz; Michael F. Shlesinger

• Publisher: Elsevier Science
• Year: 2000
• Tongue: English
• Weight: 328 KB
• Volume: 86
• Category: Article
• ISSN: 0167-7322
• DOI: 10.1016/s0167-7322(99)00137-3

✦ Synopsis

A protein is composed of a linear chain of amino acids, called its primary structure. Each amino acid has a measured hydrophobicity that reflects its attraction to or repulsion from a water environment. Going along a protein's amino acid chain the hydrophobicity sequence is analogous to a discrete data series. We analyze this data series with several numerical methods. In this paper, we will focus on decomposing this data series into orthogonal modes and then calculate the power spectrum of these modes. We find that proteins that bind together possess the same distinguishing spectral features in their power spectrum.