Molecular Conformation of Tetragastrin in Aqueous Solution by the Monte-Carlo Simulation

A conformational analysis of tetragastrin in an aqueous solution was carried out by a Monte-Carlo simulation, assuming a molecular model in a continuous media. The hydration energy of the peptide was evaluated from a calculations of the peptide–water accessible surface area. The tetrapeptide conformers in the low-energy state take an extended form, in which the two aromatic rings on both termini of the peptide are apart. The extended conformation in which the hydrophilic portions are exposed to solvent water is quite different from that in DMSO.