22 April 2024 | Furqan Dar, Samuel R. Cohen, Diana M. Mitrea, Aaron H. Phillips, Gergely Nagy, Wellington C. Leite, Christopher B. Stanley, Jeong-Mo Choi, Richard W. Kriwacki, Rohit V. Pappu
Biomolecular condensates are complex, spatially inhomogeneous network fluids formed by macromolecules, such as nucleolar granular components (GCs). These condensates exhibit a coexistence of liquid- and gas-like macromolecular densities, leading to bimodal internal molecular dynamics. The study combines small-angle neutron scattering (SANS), fluorescence recovery after photobleaching (FRAP), and coarse-grained molecular dynamics simulations to characterize the structural properties of model condensates formed by N130 and rpL5. The results show that these condensates have network-like internal organization, with spatial inhomogeneities across different length scales. The network-like structure is driven by multivalent interactions between protein and peptide domains, and is similar to network fluids formed by systems such as patchy or hairy colloids. The study also reveals that condensates formed by multivalent proteins share features with network fluids formed by systems such as patchy or hairy colloids. The findings suggest that condensates formed by multivalent proteins have network-like internal organization, with spatial inhomogeneities that reflect the contributions of distinct protein and peptide domains. The study also shows that the condensates exhibit two distinct dynamical regimes: superdiffusive at short timescales and subdiffusive at long timescales. These results highlight the importance of multivalency in driving condensation and material properties of condensates. The study also demonstrates that the network-like organization of condensates can be characterized by graph-theoretic analysis, revealing bipartite network structures with distinct interaction modules. The findings suggest that condensates formed by multivalent proteins have network-like internal organization, with spatial inhomogeneities that reflect the contributions of distinct protein and peptide domains. The study also shows that the condensates exhibit two distinct dynamical regimes: superdiffusive at short timescales and subdiffusive at long timescales. These results highlight the importance of multivalency in driving condensation and material properties of condensates.Biomolecular condensates are complex, spatially inhomogeneous network fluids formed by macromolecules, such as nucleolar granular components (GCs). These condensates exhibit a coexistence of liquid- and gas-like macromolecular densities, leading to bimodal internal molecular dynamics. The study combines small-angle neutron scattering (SANS), fluorescence recovery after photobleaching (FRAP), and coarse-grained molecular dynamics simulations to characterize the structural properties of model condensates formed by N130 and rpL5. The results show that these condensates have network-like internal organization, with spatial inhomogeneities across different length scales. The network-like structure is driven by multivalent interactions between protein and peptide domains, and is similar to network fluids formed by systems such as patchy or hairy colloids. The study also reveals that condensates formed by multivalent proteins share features with network fluids formed by systems such as patchy or hairy colloids. The findings suggest that condensates formed by multivalent proteins have network-like internal organization, with spatial inhomogeneities that reflect the contributions of distinct protein and peptide domains. The study also shows that the condensates exhibit two distinct dynamical regimes: superdiffusive at short timescales and subdiffusive at long timescales. These results highlight the importance of multivalency in driving condensation and material properties of condensates. The study also demonstrates that the network-like organization of condensates can be characterized by graph-theoretic analysis, revealing bipartite network structures with distinct interaction modules. The findings suggest that condensates formed by multivalent proteins have network-like internal organization, with spatial inhomogeneities that reflect the contributions of distinct protein and peptide domains. The study also shows that the condensates exhibit two distinct dynamical regimes: superdiffusive at short timescales and subdiffusive at long timescales. These results highlight the importance of multivalency in driving condensation and material properties of condensates.