Articles in peer-reviewed journals
|A model of solvation of polypeptide side chains. Application to angiotensin II|
|Collet O., Premilat S.|
|Journal of Molecular Structure: THEOCHEM 363 (1996) 151|
|DOI : 10.1016/0166-1280(95)04433-7|
A method is proposed to model the conformation of molecular chains taking into account solvent effects, and is applied to polypeptides of varying length and to the peptide hormone angiotensin II. The contribution of hydration to the free energy of conformation of the macromolecule is determined using the atomic accessible surface area method. A Monte Carlo sampling is performed in order to calculate the averages of structural properties of polypeptide chains in interaction with a solvent. The solvation parameters of side chains are varied from -0.2 to 0.2 kcal mol-1 AÌS-2, and the resulting solvent effects are described. The proposed model of solvation gives a good insight into the way in which modifications of molecular conformations are induced by the transfer of polypeptide chains from an aqueous solvent to an apolar medium.