The structural analysis of the
deuterated proteins is considered to be the main source for the crystallography
process, which involves refinement of X-ray while using atomic and molecularthermal stability factors. These thermal stabilities get affected sometimes due
to the masses of hydrogen and deuterium atoms. Further, this method has been
applied to analyse the deuterium exchanging of protein crystals.
It is important in the structural
analysis of protein tertiary structures to determine the positions of hydrogen
atoms and solvent water. For example, the catalytic sites of enzymes include
specific hydrogen atoms that are essential to their catalytic mechanisms. This information has contributed to progress in chemical biology, pharmacy, andmedical sciences. Neutron diffraction is a powerful technique to determine the
positions of hydrogen atoms in a protein molecule with high precision, although
it is necessary to crystallize the deuterated protein because of decreasing
incoherent scattering from the many hydrogen atoms in a protein molecule.