The　theoretical　and　experimental　studies　have　showed　that　the　topology　of　the　native　structure　of　protein　plays　an　important　role　in　determining　its　folding　process.　The　complex　network　approach　was　used　to　analyze　the　topological　characters　of　the　native　structure　of　protein　and　then　explore　the　relationship　between　these　characters　and　the　experimental　folding　rates.　Several　types　of　network　were　constructed,　including　all-amino-acids　network,　hydrophobic　amino　acid　network,　hydrophilic　amino　acid,　hydrophobic-hydrophilic　amino　acid　network　and　their　corresponding　long-range　interaction　network.　The　statistic　characters　of　the　assortativity　coefficient　and　the　clustering　coefficient　were　studied.　The　results　indicate　that　all　types　of　network　except　for　the　hydrophobic-hydrophilic　one　are　of　the　positive　assortativity　coefficient.　Furthermore,　there　is　an　obvious　linear　positive　correlation　between　the　assortativity　coefficient　and　the　folding　rate　for　the　all　amino　acids　network　and　the　hydrophobic　amino　acid　network,　which　implies　that　the　cooperative　interactions　of　the　hydrophobic　amino　acids　are　important　for　proteins　rapidly　folding　into　their　native　states.　Moreover,　it　is　found　that　there　is　a　clear　linear　negative　correlation　between　the　clustering　coefficient　of　the　hydrophobic　amino　acid　networks　and　the　experimental　folding　rates　of　the　corresponding　proteins,　which　indicates　that　the　formation　of　the　triangle　construction　among　the　amino　acids　reduces　the　folding　rates.　It　is　also　found　that　in　the　long-range　interaction　networks,　the　formation　of　contact　pairs　linking　two　distant　residues　in　sequence　would　slow　down　the　process　of　protein　folding.