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Specific interactions for ab initio folding of protein terminal regions with secondary structures
Author(s) -
Yang Yuedong,
Zhou Yaoqi
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21968
Subject(s) - folding (dsp implementation) , protein folding , ab initio , chemistry , dipole , crystallography , lattice protein , protein secondary structure , protein structure , molecule , amino acid , orientation (vector space) , biophysics , biochemistry , biology , geometry , organic chemistry , electrical engineering , engineering , mathematics
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.