Simulations of reversible protein aggregate and crystal structure

摘要: We simulated the structure of reversible protein aggregates as a function surface characteristics, protein-protein interaction energies, and entropic penalty accompanying immobilization in solid phase. These simulations represent an extension our previous work on kinetically irreversible aggregate are based explicit accounting specific interactions that occur within crystals. considered monomers with mixture hydrophobic hydrophilic regions suspended polar solvent; energetic driving force for aggregation is provided by burial solvent-exposed area. analyzed physical properties generated aggregates, including density, contact distributions, solvent accessible area, porosity, order, compared results crystallization literature well case. The were consonant those observed although general, more stable energetically crystal-like their order content than counterparts. less dense indicating increased stability derived primarily from optimality rather density packing extent contacts area phase depended pathway: tended to have greater proportion hydrophobic-hydrophobic smaller fraction Furthermore, arrangement patches played major role distribution content. This was readily reflected aggregates: contiguity monomer surface, ordered became, despite opportunities rearrangement offered pathway. enhanced understanding impact structural motifs demarcation between crystallization.