Fractal aggregates in protein crystal nucleation.
Monte Carlo simulations of homogeneous nucleation for a protein model with an exceedingly short-ranged attractive potential yielded a nonconventional crystal nucleation mechanism, which proceeds by the formation of fractal, low-dimensional aggregates followed by a concurrent collapse and increase of the crystallinity of these aggregates to become compact ordered nuclei. This result corroborates a recently proposed two-step mechanism for protein crystal nucleation from solution.
Chen
Bin
B
Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803-1804, USA. binchen@lsu.edu
Nellas
Ricky B
RB
Keasler
Samuel J
SJ
D003198:Computer Simulation; D003460:Crystallization; D008956:Models, Chemical; D009010:Monte Carlo Method; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry
D011506:Proteins; D012996:Solutions