|Hoogerheide, David P
At the NIST Center for Neutron Research, neutron scattering is routinely used to study solutions and surface adsorption of biomacromolecules. Neutrons are particularly well suited to study biological materials because of their sensitivity to light constituent elements, such as H, C, and N. In combination with simulation, complementary biophysical techniques such as surface plasmon resonance, and advanced data analysis techniques, neutron reflectivity has proven to have unique advantages for studying the structural biology of proteins on biomimetic bilayer lipid membrane (BLM) surfaces under physiologically relevant conditions. Successful projects have featured studies of intrinsically disordered proteins, determination of the structure of a membrane-bound protein complex, and manipulation of membrane-bound protein structure.
The bioreflectometry group collaborates with academic and various government laboratories to elucidate mechanisms of protein binding to BLMs. We comprise researchers with a broad range of expertise and are actively developing advanced biochemical and biophysical techniques, particularly those useful for neutron scattering, to study membrane-associated proteins. We are interested in chemistries for new measurement platforms, protein synthesis and diagnostics; advanced data analysis techniques; instrument and sample environment development; and simulation methods to compare to experimental results.
Barros M, et al: Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation. Journal of Virology 90(9): 4544-4555, 2016
Heinrich F, Losche M: Zooming in on disordered systems: neutron reflection studies of proteins associated with fluid membranes. Biochimica et biophysica acta 1838(9): 2341-2349, 2014
Nanda H, Heinrich F, Losche M: Membrane association of the PTEN tumor suppressor: Neutron scattering and MD simulations reveal the structure of protein-membrane complexes. Methods 77-78: 136-146, 2015
Binding (biochemical); Lipid bilayers; Membrane proteins; Neutron reflectivity; Molecular dynamics simulations; Biophysical techniques; Surface plasmon resonance; Tethered bilayer lipid membranes;