Recent calorimetric measurements of the solvation enthalpies of some dipeptide analogs confirm our earlier prediction that the principle of group additivity is not valid for the interaction of the peptide group with water. We examine the consequences for understanding the properties of peptide solvation. A major consequence is that the current value of the peptide solvation enthalpy, which is a basic parameter in analyzing the energetics of protein folding, is seriously wrong. Electrostatic calculations of solvation free energies provide an estimate of the size and nature of the error.
COBISS.SI-ID: 4103962
The NMR studies and molecular dynamics simulations of ligand-MurD complexes have been performed to obtain the insight into dynamic properties of novel complexes, which can significantly upgrade the drug design studies that are based solely on the static crystal structures. The results revealed the differing degrees of ligand flexibility and their effect on particular ligand-enzyme contacts. The degree of conformational flexibility depends on the specificity of the ligand molecular structure and can be related to the differences in their inhibitory activities.
COBISS.SI-ID: 4121626