00000ctm a22000003a 4500 UP-1685594773861970264 Buklod 20140913101806.0 g||| | || || ta 200608s2014 xx a rbm |||| u|eng d (iLib)UPBAG-00014758860 BAG rda eng Thesis Castro, Benedict Z. author. Random coil formation for protein primary structures via self-avoiding random walk model Benedict Z. Castro. 2014. x, 53 leaves color illustrations 29 cm text rdacontent unmediated rdamedia volume rdacarrier Thesis (Bachelor of Science) -- University of the Philippines Baguio, 2014. Includes bibliographical references (leaves 49-53). The initial folding states of three different protein test structure, Pheromone ER-1, Pheromone ER-10, and Pheromone ER-22, in their primary states are modelled using the self-avoiding random walk embedded in a lattice. Different Bravias lattices were used to assess the effect of the coordination number. A lattice with a high coordination number is also observed to minimize one disadvantage of lattice models, which is the possibility of the walker being trapped in its own steps. For conformational entropy considerations, all lattice types yield average conformational entropy values, which fit well with available experimental data. In the context of the Hydrophobic-Polar (HP) model, the FCC lattice is the one recommended for modelling purposes because it yields the lowest observed HP free energy compared to other lattices used in this study. Due to limited protein data resources, other parameters obtained in the models cannot be efficiently tested for real protein data fitting. But still, general insights about the effect of different lattice models to protein structure properties are great importance. -- Author's abstract. Protein folding Computer simulation. UP UPBAG UPBAG-MAIN Thesis Thesis