Computer Simulation of Biomolecular systems
Structural peculiarities of water in different regions
of biomolecular hydration may play a key role in many biochemical processes.
The aqueous solution of tuftsin (Thr-Lys-Pro-Arg, residues 289-292 of leukokinin,
a cytophilic g-globulin that stimulates the phagocytosis) is studied using
extended molecular dynamics simulations on a nanosecond time scale.
Water structure around hydrophobic and polar groups of tuftsin has been
analyzed using statistical geometry approach and more conventional structural
descriptors. Specificity of water structure in different hydration
regions is better reflected by the distribution of tetrahedrality of Delaunay
simplexes and angular orientation of water molecules with respect to the
solute rather than by distributions of hydrogen bond distances, angles,
and energies. Various correlations between conformational behavior of tuftsin
and water structure in its hydration shell are studied in this project.