Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling.

摘要: The biological small-angle neutron scattering instrument at the High-Flux Isotope Reactor of Oak Ridge National Laboratory is dedicated to investigation materials, biofuel processing, and bio-inspired materials covering nanometer micrometer length scales. methods presented here for investigating physical properties (i.e., size shape) membrane proteins (here, MmIAP, an intramembrane aspartyl protease from Methanoculleus marisnigri) in solutions micelle-forming detergents are well-suited this instrument, among others. Other biophysical characterization techniques hindered by their inability address detergent contributions a protein-detergent complex structure. Additionally, access Bio-Deuteration Lab provides unique capabilities preparing large-scale cultivations expressing deuterium-labeled enhanced signal protein. While technique does not provide structural details high-resolution, knowledge gap contains many addressable areas research without requiring near-atomic resolution. For example, these include determination oligomeric states, formation, conformational changes during perturbation, folding/unfolding events. These investigations can be readily accomplished through applications method.