Exactly solvable model for helix-coil-sheet transitions in protein systems.
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.
Schreck
John S
JS
Department of Physics, Drexel University, Philadelphia, Pennsylvania 19104, USA. jss74@drexel.edu
Yuan
Jian-Min
JM
D000465:Algorithms; D001703:Biophysics / Q000379:methods*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D015233:Models, Statistical; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012997:Solvents; D013696:Temperature; D013816:Thermodynamics
D010455:Peptides; D011108:Polymers; D011506:Proteins; D012997:Solvents