M. Ramanadham et al., HYDROGEN-BONDING, NEUTRON-DIFFRACTION AND BIOMOLECULAR STRUCTURE AND FUNCTION, Indian Journal of Pure & Applied Physics, 35(11), 1997, pp. 722-728
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.