Membrane fusion between the virus envelope and host cells is the first step of the enveloped virus entry into the host cells. This process involves the interaction of viral envelope proteins and their cellular receptors (proteins or sialic aids), which leads to the conformational changes of the envelope proteins. Avian paramyxovirus-2 (APMV-2) has the hemagglutinin- neuraminidase (HN) glycoprotein in which there are the stalk and globular head regions, and the fusion (F) glycoprotein in which there are the heptad repeat 1 (HR1) and heptad repeat 2 (HR2) and heptad repeat 3 (HR3) regions. To construct and express the correlative genes with membrane fusion of APMV-2 ， the relative sequences basing on the published sequences of avian paramyxovirus-1 (APMV-1) and using BLAST bio-software were ensured, then constructed genes by PCR and cloned genes into the BamHⅠ-XhoⅠ restriction sites of the GST fusion expression vector pGEX-6P-I, in which there is a rhinovirus 3C protease cleavage site for the fusion protein. E. coli strain BL21 (DE3) was transformed with the recombinant GST fusion plasmids. The supernatants lysed by sonication and clarified by centrifugation were passed over Glutathione-Sepharose 4B column for purifying, respectively. The GST fusion proteins were then cleaved by GST-fusion rhinovirus 3C protease and then were purified by the affinity chromatography. The LearnCoil-VMF and ExPASy bio-softwares were used for predict and analysis the structure and function of five peptides. And the results of Gel-filtration and circular dichroism (CD) showed that the HR1 and HR2 form a six-helix structure.