I investigate a disordered version of a simplified model of protein folding, with binary degrees of freedom, applied to an ideal beta-hairpin structure. Disorder is introduced by assuming that the contact energies are independent and identically distributed random variables. The equilibrium free energy of the model is studied, by performing the exact calculation of its quenched value and proving the self-averaging feature.
An exactly solvable model for a beta-hairpin with random interactions
Zamparo, M
2008-01-01
Abstract
I investigate a disordered version of a simplified model of protein folding, with binary degrees of freedom, applied to an ideal beta-hairpin structure. Disorder is introduced by assuming that the contact energies are independent and identically distributed random variables. The equilibrium free energy of the model is studied, by performing the exact calculation of its quenched value and proving the self-averaging feature.File in questo prodotto:
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