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Abstract: In view of the important role helix-sheet transitions play in proteinaggregation, we introduce a simple model to study secondary structuraltransitions of helix-coil-sheet systems using a Potts model starting with aneffective Hamiltonian. This energy function depends on four parameters thatapproximately describe entropic and enthalpic contributions to the stability ofa polypeptide in helical and sheet conformations. The sheet structures involvelong-range interactions between residues which are far in sequence, but are incontact in real space. Such contacts are included in the Hamiltonian. Usingstandard statistical mechanical techniques, the partition function is solvedexactly using transfer matrices. Based on this model, we study thermodynamicproperties of polypeptides, including phase transitions between helix, sheet,and coil structures.



Author: John S. Schreck, Jian-Min Yuan

Source: https://arxiv.org/







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