Interface-induced protein unfolding on hydrophobic and polar interfaces was studed using a two-dimensional lattice model. It was suggested that the unfolding proceeds by a large, sudden loss of native contacts. The results show that the unfolding at polar interfaces exhibits similar behavior to that at hydrophobic interfaces but with a much weaker interface coupling strength. It was also found that the resistance of proteins to unfolding in the model is positively correlated with the magnitude of the folding energy in the native-state structure, energy gap for that structure and the interface energy for native-state adsorption.
|Journal||Physical Review E - Statistical, Nonlinear, and Soft Matter Physics|
|Issue number||2 1|
|State||Published - Feb 2004|