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Exactly solvable model for helix-coil-sheet transitions in protein systems
Journal article   Open access

Exactly solvable model for helix-coil-sheet transitions in protein systems

John S. Schreck and Jian-Min Yuan
Physical review. E, Statistical, nonlinear, and soft matter physics, v 81(6), pp 061919-061919
17 Jun 2010
PMID: 20866452
url
http://arxiv.org/abs/1005.4919View

Abstract

Physical Sciences Physics Physics, Fluids & Plasmas Physics, Mathematical Science & Technology
In view of the important role helix-sheet transitions play in protein aggregation, we introduce a simple model to study secondary structural transitions of helix-coil-sheet systems using a Potts model starting with an effective Hamiltonian. This energy function depends on four parameters that approximately describe entropic and enthalpic contributions to the stability of a polypeptide in helical and sheet conformations. The sheet structures involve long-range interactions between residues which are far in sequence, but are in contact in real space. Such contacts are included in the Hamiltonian. Using standard statistical mechanical techniques, the partition function is solved exactly using transfer matrices. Based on this model, we study thermodynamic properties of polypeptides, including phase transitions between helix, sheet, and coil structures.

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Web of Science research areas
Physics, Fluids & Plasmas
Physics, Mathematical
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