Modeling the solvation of peptides. The case of (s)-N-acetylproline amide in liquid water.

The structure and properties of (s)-N-acetylproline amide (NAP) in aqueous solution are studied by exploiting a continuum solvation model. The conformational preference of NAP as a function of the environment is discussed as well as data for a number of chiral and non-chiral spectroscopic and response properties (IR/VCD, Raman/VROA, UV/CD, ORD, NMR), whose calculation with the accounting of solvent effects is now possible due to recent developments introduced in the PCM approach. When available, calculated results are compared with experimental data, so as to evaluate the quality of the continuum approach to the solvation of this system.