title: Deuteration in Biological Neutron Reflectometry.
abstract: Neutron reflectometry (NR) is uniquely positioned in structural biology, because of its ability to characterize biomolecular interfacial architectures like lipid membranes and membrane-associated proteins nondestructively 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 NR 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 overinterpretation. This is achieved by employing robust methods for the determination of modeling uncertainties. Integrative modeling approaches for NR are emerging as an essential part of the technique.
authors.affiliation: Department of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA; Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland, USA. Electronic address: fheinrich@cmu.edu.
authors.forename: Frank
authors.initials: F
authors.lastname: Heinrich
mesh_terms: D002462:Cell Membrane / Q000737:chemistry; D003903:Deuterium / Q000737:chemistry*; D041961:Deuterium Exchange Measurement; D008051:Lipid Bilayers / Q000737:chemistry; D046911:Macromolecular Substances / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D009502:Neutrons; D013194:Staining and Labeling / Q000379:methods*
chemical_list: D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008565:Membrane Proteins; D003903:Deuterium
keywords: Biological neutron reflectometry; Composition space modeling; Deuteration; Membrane proteins; Protein complexes