EFFECTS OF SOLVENT ON THE CONFORMATION AND THE COLLECTIVE MOTIONS OF A PROTEIN .2. STRUCTURE OF HYDRATION IN MELITTIN

The dynamic correlation of solvent molecules with the collective motions of a protein is studied on the basis of a molecular dynamics simulation. Our attention is focused especially on the response of the solvent molecules to the conformational transition of the protein, which has been observed in a 50-psec trajectory projected onto low-frequency collective modes (Chem. Phys. 1991, 158, 447). It is shown that the conformational transition is associated with an extensive change in the atom packing and the-hydrogen-bond network between protein and water molecules.