| 초록 |
At native state of protein, large portion of occluded surface and inner volume were investigated to exist in buried part of a protein. To consider the influence of occluded surface and inner volume to protein conformational stability, inner solvation energy concept was introduced to conventional solvation model. Inner solvation energy was proportional with occluded surface, and its strength was specified by inner atomic solvation parameter and correct parameter, which indicate the inner volume. Folding energy calculated by packing-considered solvation energy model was negatively proportional with number of protein residues as like those of other conventional solvation models. However, packing-considered solvation energy model could discriminate correct folded form in 25 native/decoy set more accurately than other solvation energy models. This model would be useful for prediction of hydrophobic contribution to protein structure and could be suitable for evaluation of protein conformational stability. |
