Biochemistry Seminar: Laura R. Stingaciu: The Neutron Spin Echo Spectrometer at SNS and Its Biophysics Applications
Laura R. Stingaciu, Instrument Scientist, SNS-NSE Neutron Sciences, Oak Ridge National Laboratory, will give a talk on "The Neutron Spin Echo Spectrometer at SNS and Its BIophysics Applications."
Given the state of human diseases development, with viruses and bacterial strain more and more resistant to drugs treatments and spontaneous genetic mutations that alter the proper functionality of genes, it is imperative that alternatives are found to classical peptides synthesis for treatment purposes. Antibodies (Ig) are large Y-shaped molecules produced by the humoral immune system that consist of three equal sized domains connected by flexible linker regions. The internal dynamics of human monoclonal antibodies is of a particular importance for the detection, recognition and formation of antibody-antigen complexes. Our research focused on refining the internal dynamics of these large multi-domain flexible proteins using experimental scattering methods SAXS (small-angle-Xray scattering), SANS (small-angle neutron scattering), and NSE (neutron spin echo spectroscopy) combined with computer modeling and simulations. We aimed to identify the correct time scale of the domains motions and their response to protein environmental conditions in order to understand and access the biomechanics of the docking sites. The ability to temper with binding and docking sites domains in antibody proteins will give us the opportunity to include specific details of the domain dynamics within new complexes and create unique classes of protein that will help to develop improved strategies for drug design. The neutron techniques and the mathematical models applied to describe the domain dynamics of antibodies can also be successfully used to investigate different classes of proteins like intrinsically disordered proteins.