Abstract
Hydrogen has a strong polarization-dependent neutron scattering cross section. This property has been exploited in the study of soft matters, especially biological macromolecules. When a polarized neutron beam is scattered off a polarized hydrogenous sample, the otherwise large hydrogen incoherent cross section is drastically reduced while the coherent signal is significantly increased. Past experiments have demonstrated the potentials and benefits of polarized neutron scattering from soft materials. The main technical challenge of polarized neutron scattering from biological matters lies at sample polarization. Dynamic nuclear polarization is a proven yet rather sophisticated technique. Its complexity is one of the main reasons for the technique's slow adoption. The future of polarized neutron scattering in biology may rest largely in neutron protein crystallography. Polarization of protein crystals is much easier to accomplish, since protein crystals are typically rather small (<<1 mm) and only require small and easy- to-operate polarization apparatuses. In addition, the high resolution nature of neutron protein crystallography means that we will be able to study individual atoms using the polarized neutron scattering technique.
