Continuity of Short-Time Dynamics Crossing the Liquid–Liquid Phase Separation in Charge-Tuned Protein Solutions
Year: 2024
Type: article
Abstract: Liquid-liquid phase separation (LLPS) constitutes a crucial phenomenon in biological self-organization, not only intervening in the formation of membraneless organelles but also triggering pathological protein aggregation, which is a hallmark in neurodegenerative diseases. Employing incoherent quasi-elastic neutron spectroscopy (QENS), we examine the short-time self-diffusion of a model protein undergoing LLPS as a function of phase splitting and temperature to access information on the nanosecond hydrodynamic response to the cluster formation both within and outside the LLPS regime. We investigate the samples as they dissociate into microdroplets of a dense protein phase dispersed in a dilute phase as well as the separated dense and dilute phases obtained from centrifugation. By interpreting the QENS results in terms of the local concentrations in the two phases determined by UV-vis spectroscopy, we hypothesize that the short-time transient protein cluster size distribution is conserved at the transition point while the local volume fractions separate.
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $4,500
Awards: G1696892011, Von BATS zu MIRACLES: Die Zukunft der hochauflösenden Neutronenrückstreuspektroskopie in Europa, G3655483235, G3964588663, G4220268679, Dynamics, kinetics and assembly of model intrinsically disordered proteins from a polymer physics perspective, Static and dynamic properties of antibody proteins in solution - the effects of crowding and charge-tuning, G6774927082, Vollständiger Ausbau der BATS Option für IN16B, G8897267886
OpenAlex ID: W4404748768