#24 · Structural bio & protein design

Architecture steers interface outcomes in condensates, membranes, actin, and receptors

The dominant thread is that architectural variables condition interaction outcomes in molecular dynamics of biomolecular interfaces. In coarse-grained simulations, cation-π interactions stabilize heterotypic condensates, promoting mixing and suppressing heterogeneity in local structure and dynamics. All-atom comparison of tetra-branched SET-M33 with linear Q33 shows that branching suppresses self-aggregation while preserving surface membrane binding. SMD simulations and force spectroscopy show that C-terminal pulling unfolds cellulosomal CBM3a before unbinding from cellulose, whereas N-terminal pulling does not. Coarse-grained and all-atom simulations indicate that VASP anchors the lateral actin subunit, stabilizing early actin nuclei. Constant-force pulling shows that a reconstructed GPVI dimer loses interreceptor contacts faster than domain-swapped GPVI or CLEC-2 assemblies. What is new is the pairing of structural variables with a functional readout across distinct systems, although the studies differ in method, scale, and system.