Structural properties of hydration shell around various conformations of simple polypeptides.

In this paper we investigate structural properties of water within the solvation shell around the peptide core created by a well-defined conformation of polypeptide chain. The following secondary structures are investigated: linear (straight chain), and three helices PII (polyproline-like), 3(10), and alpha. We propose using the two-particle contribution to entropy as a rational measure of the water structural ordering within the solvation layer. This contribution divides into two terms, depending on the peptide-water and water-water interactions, respectively, and in this paper both terms are investigated. The structure of "solvation" water is described by the second term, and therefore it mainly attracts our attention. Determination of this term, however, is not an easy task, requiring some controversial approximations. Therefore, we have transformed this term to the form of some rational parameter which measures the local structural ordering of water within the solvation shell. Moreover, the results of several independent investigations are reported: we adopt the harmonic approximation for an independent estimation of the water entropy within the solvation shell, and we also study structure of the water-water hydrogen bond network, mean geometry of a single hydrogen bond, the self-diffusion coefficients (both translational and rotational) of water, and the mean lifetimes of water-water and water-peptide hydrogen bonds. All the obtained results lead to the conclusion that the local structure of water within the solvation shell changes only slightly in comparison to the bulk one. If so, the measure of local water ordering proposed by us is exploited with the aim to gain the deeper insight on the structural properties of "solvation" water. It has been shown that this parameter can be factored into three terms, which measure translational, configurational, and orientational ordering, respectively. Using this factoring, the ordering map for a precise description of the water local ordering has been built. An interesting correlation is observed: the points on this map lie approximately on the straight line, while the linear conformations clearly deviate from the general tendency. Further analysis of the obtained results allows us to express the supposition that an increasing local ordering of water around given secondary structure corresponds to an increasing relative stability of this structure in aqueous solution. Analyzing the geometry of the water-water hydrogen bond network within the solvation layer, we find some systematic deviations of this geometry from the bulk water properties. We also observe that the alanine peptides (excluding the linear form) disturb the hydrogen bond network in the less range, and in another way than the various conformations of polyglycine, while the linear form of polyalanine behaves very similarly to the glycine ones. Next, investigating the dynamic properties, we also conclude that water near the peptide surface creates a pseudorigid structure, a "halo" around the peptide core. This "halo" is stabilized by slightly higher energy of the hydrogen bonds network: we have found that within this region the hydrogen bonds network is slightly less distorted, the water-water hydrogen bonds are a little more stable and their mean lifetime is clearly longer that that of bulk water. Significant differences between the alanine- and glycine-based polypeptides are also visible. It has also been found that this solvation layer interacts with the polyalanine in another way than with polyglycine. Although in the case of the glycine-based polypeptide this layer slides relatively freely over the peptide surface, for the alanine-based polypeptide this sliding is strongly hindered by the presence of the methyl groups, and this effect is additionally enhanced by a rise in the solvation layer rigidity. Thus, the survey of various dynamic properties allows us to perceive and to explain distinct differences in behavior of water within the solvation shell around both glycine and alanine peptides.