Protein self-organization is a key reaction in downstream biotechnology, as protein refolding is always the bottleneck of producing recombinant protein in bacterial cell, and in vitro assembly of virus-like particles (VLPs) is crucial for producing new vaccines and carrier for drug delivery and gene therapy. Correct folding and assembly reaction always compete with aggregation, so mixing effect in reactor will influence the reaction rate as well as the product distribution among different species. The role of mixing on dilution protein refolding has recently been understood, though how dispersion in chromatographic column influence protein self-organization has not been reported. Here we report that chromatographic refolding yield is influenced strongly by column dispersion; experimental yield could be increased from 28% to 46% simply by increasing the column flowrate from 0.2 mL min^-1 to 3.0 mL min^-1 (corresponding to superficial velocities of 0.43 and 6.37 x 10^-4 m s^-1). By counter-intuitively introducing a 15 mm highly-dispersive gap at the top of the column (i.e., between the inlet distributor and the top of the packed chromatographic bed), the yield was increased to 66% at 3.0 mL min^-1. Such mixing effect influencing the product distribution for VLP assembly reaction in chromatography column reactor is also reported.