Fast global and internal dynamics of the NIST monoclonal antibody
Monoclonal antibodies (mAbs) bind very selectively to different antigens and mAbs are used nowadays as molecularly engineered pharmaceuticals. Successful mAb applications that allow for facile home administration require stable and low viscosity formulations with high mAb concentration, which are often difficult to achieve. The complexity of the system, formed by anisotropic and flexible large molecules that interact through several different intermolecular forces leads to various macroscopic phenomena. In the proposal for IN16B we would like to explore global protein self-diffusion in the short-time limit and internal motions of the NIST mAb using high-resolution quasielastic neutron scattering (QENS). We suggest studying the effect of concentration and temperature on short-time self-diffusion of the NIST mAb with the aim to investigate the fundamental correlation between macroscopic solution viscosity, protein flexibility (domain motions, rotational diffusion) as probed by NSE and their inherent connection to short-time self-diffusion. Furthermore, QENS would allow us to access larger q-vectors and probe faster local internal motions than what is currently available with NSE.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
Andreas M. Stadler; APPEL Markus; BIEHL Ralf; KRUTEVA Margarita; POLIMENI Marco; SARINGER Szilard; SCHURTENBERGER Peter; SEYDEL Tilo and STRADNER Anna. (2023). Fast global and internal dynamics of the NIST monoclonal antibody. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-955
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This data is not yet public
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