<abstract>
<p>Many of the simplistic hydrophobic-polar lattice models, such as Dill's model (called <bold>Model 1</bold> herein), are aimed to fold structures through hydrophobic-hydrophobic interactions mimicking the well-known hydrophobic collapse present in protein structures. In this work, we studied 11 designed hydrophobic-polar sequences, S<sub>1</sub>-S<sub>8</sub> folded in 2D-square lattice, and S<sub>9</sub>-S<sub>11</sub> folded in 3D-cubic lattice. And to better fold these structures we have developed <bold>Model 2</bold> as an approximation to convex function aimed to weight hydrophobic-hydrophobic but also polar-polar contacts as an augmented version of <bold>Model 1</bold>. In this partitioned approach hydrophobic-hydrophobic ponderation was tuned as <italic>α</italic>-1 and polar-polar ponderation as <italic>α</italic>. This model is centered in preserving required hydrophobic substructure, and at the same time including polar-polar interactions, otherwise absent, to reach a better folding score now also acquiring the polar-polar substructure. In all tested cases the folding trials were better achieved with <bold>Model 2</bold>, using <italic>α</italic> values of 0.05, 0.1, 0.2 and 0.3 depending of sequence size, even finding optimal scores not reached with <bold>Model 1</bold>. An important result is that the better folding score, required the lower <italic>α</italic> weighting. And when <italic>α</italic> values above 0.3 are employed, no matter the nature of the hydrophobic-polar sequence, banning of hydrophobic-hydrophobic contacts started, thus yielding misfolding of sequences. Therefore, the value of <italic>α</italic> to correctly fold structures is the result of a careful weighting among hydrophobic-hydrophobic and polar-polar contacts.</p>
</abstract>
Influence of substrate pattern on the adsorption of HP lattice proteins
