1.

Confirmation of our hypothesis that the principle of group additivity of peptide groups cannot be used to study thermodynamics of protein folding.

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

2.

New insight into design of antibacterial drugs based on structure-dynamic studies of complexes of novel ligands with MurD ligase.

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

3.

Identification of hydrogen bond modes in polarized Raman spectra of single crystals of [alpha]-oxalic acid dihydrate.

Polarized Raman spectra of single crystals of the ?-polymorphs of oxalic acid dihydrate were recorded. The interpretation of the spectra is assisted by the periodic DFT calculation using the CRYSTAL06 program and by comparison with the IR spectra. The agreement between the calculated and observed band frequencies is fair in the case of low anharmonicity modes. Deuteration does not notably affect the frequency limits of the broad OH(D) stretching band; this suggests that the potential governing the proton dynamics is of the asymmetric double minimum type with a very low barrier.

COBISS.SI-ID: 4189210

4.

Experimental evidence of long-range hydration force in phospholipids bilayers.

We probed the effect of multi-bilayer lipid films on the structure and dynamics of inter-lamellar water between bilayers by using by using infrared spectroscopy. H-bonding is weakened in water between lipid bilayers in excess water. Moreover, the water structure is perturbed throughout the inter-lamellar space. Our results imply that besides repulsive short range hydration force, another long-range contribution to the hydration force due to the restructuring of inter-lamellar water at larger inter-lamellar distances should be added.

COBISS.SI-ID: 22670631

5.

Role of lipid bilayers on valsartan - AT1 receptor interactions.

Binding interactions of valsartan, a potent antihypertensive drug, with membrane embedded AT1 receptor have been determined by application of NMR spectroscopy of valsartan in solvent environment and theoretical simulations of molecular dynamics of valsartan-AT1 receptor complex in lipid bilayer environment. Enhancement of binding interactions and stabilization of drug at the active site upon membrane environment have been observed pointing to a crucial role of lipid bilayers in the mechanism of action of AT1 antagonist.

COBISS.SI-ID: 4115994