HYDROGEN-BONDING, NEUTRON-DIFFRACTION AND BIOMOLECULAR STRUCTURE AND FUNCTION

The hydrogen bond interaction is one of the most vital non- covalent i nteractions in determining the structure and physico- chemical propert ies of matter, especially those of biological macromolecules, such as DNA and proteins. Neutron diffraction is the method of choice to study the geometry of H-bond interaction in crystal structures of hydrogen bonded systems. Analysis of high-precision neutron studied on amino ac ids, small peptides, etc., provides useful data on H-atom stereochemis try and H-bond geometry. This information is used to analyse and inter pret a few functional aspects of two protein structures studied by the method of X-ray diffraction.