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Neutron reflectometry is uniquely positioned in structural biology, because of its ability to characterize biomimetic interfacial architectures like lipid membranes and membrane-associated proteins non-destructively and in their native environment. Mimicking biological processes, samples can be manipulated and their structural response can be measured. Specific deuteration is an integral part of biological neutron reflectometry as it is essential for resolving, for example, individual components of membrane-bound protein-protein complexes. Data analysis techniques have been developed in the past decade that extract the maximum structural detail from reflectivity data obtained from samples with complex deuteration schemes while avoiding over-interpretation. This is achieved by employing robust methods to determine modeling uncertainties. Integrative modeling approaches for neutron reflectometry are emerging as an essential part of the technique.
Heinrich, F.
(2015),
Deuteration in Biological Neutron Reflectometry, Methods in Enzymology, Elsevier, Rockville, MD, [online], https://doi.org/10.1016/bs.mie.2015.05.019
(Accessed December 6, 2024)