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In experiments, the free energy of transferring the peptide group from waterto an osmolyte solution is obtained using the transfer free energy of (Gly)_nwith the added assumption that a constant incremental change in free energywith n implies that each additional unit makes an independent contribution tothe free energy. Here we test this assumption and uncover its limitations.Together with results for cyclic-diglycine, we show that, in principle, it isnot possible to obtain a peptide group transfer free energy that is independentof the model system. We calculate the hydration free energy ofacetyl-(Gly)_n-methyl amide (n=1..7) peptides modeled in the extendedconformation in water and osmolyte solutions and find that the hydration freeenergy is linear in n, suggestive of independent, additive group-contributions.To probe the observed linearity further, we study the hydration of the solutebereft of water molecules in the first hydration shell. This conditioned solutearises naturally in the theoretical formulation and helps us focus on hydrationeffects uncluttered by the complexities of short-range solute-waterinteractions. We subdivide the conditioned solute into n+1 peptide groups and amethyl end group. The binding energy of each of these groups with the solventis Gaussian distributed, but the near neighbor binding energies are themselvescorrelated: the (i,i+1) correlation is the strongest and tends to lower thefree energy over the independent group case. We show that the observedlinearity can be explained by the similarity of near neighbor correlations.Implications for group additive transfer free energy models are indicated.

Examining the meaning of the peptide transfer free energy obtained from blocked (Gly)_n and cyclic-diglycine model compounds