Proteins are important biomolecules studied for many years because of their necessary function. Several models have been developed with the aim of simulating or predicting their natural three-dimensional conformation. In this work, interesting relationships between the amino acid (AA) sequence of a protein and its spontaneous folding conformations are investigated. In particular, the hydrophobicity and hydrophilicity of the amino acids are used for achieving information on the volume, surface and hydrophilic shell of the protein conformations. The presented results can be exploited in methods for protein simulation and prediction.