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Folding and dimerization of the ionic peptide EAK 16‐IV
Author(s) -
Yan Zhiqiang,
Wang Jun,
Wang Wei
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.21903
Subject(s) - electrostatics , folding (dsp implementation) , ionic bonding , chemistry , chemical physics , peptide , biophysics , electrostatic interaction , protein folding , static electricity , crystallography , ion , physics , biochemistry , biology , organic chemistry , quantum mechanics , electrical engineering , engineering
Folding and dimerization of an ionic polyalanine‐based peptide chain (EAK16‐IV) are simulated with nonspecific interactions. It is found that there is a competition between two kinds of structural motifs under different strengths of electrostatic interactions. The dominance of hairpin‐like structures would be realized with a strong electrostatic interaction both thermodynamically and kinetically, showing the importance of the electrostatic interaction on the formation of hairpin‐like structures. Simulations on the dimerization with strong electrostatic interaction are also carried out. It is found that the concentration contributes essentially to the shape of the dimers. These studies demonstrate that the strong interactions and kinetic factors might be important for the ordered amyloid aggregates. Proteins 2008. © 2008 Wiley‐Liss, Inc.