Get access

Specific interactions for ab initio folding of protein terminal regions with secondary structures

Authors

  • Yuedong Yang,

    1. Indiana University School of Informatics, Indiana University-Purdue University and Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, Indiana 46202
    Search for more papers by this author
  • Yaoqi Zhou

    Corresponding author
    1. Indiana University School of Informatics, Indiana University-Purdue University and Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, Indiana 46202
    • Indiana University School of Medicine, Walker Plaza, 719 Indiana Avenue, Suite 319, Indianapolis, IN 46202
    Search for more papers by this author

Abstract

Proteins fold into unique three-dimensional structures by specific, orientation-dependent interactions between amino acid residues. Here, we extract orientation-dependent interactions from protein structures by treating each polar atom as a dipole with a direction. The resulting statistical energy function successfully refolds 13 out of 16 fully unfolded secondary-structure terminal regions of 10–23 amino acid residues in 15 small proteins. Dissecting the orientation-dependent energy function reveals that the orientation preference between hydrogen-bonded atoms is not enough to account for the structural specificity of proteins. The result has significant implications on the theoretical and experimental searches for specific interactions involved in protein folding and molecular recognition between proteins and other biologically active molecules. Proteins 2008. © 2008 Wiley-Liss, Inc.

Ancillary