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Introduction:The proteins of the Bin/Amphiphysin/Rvs167 (BAR) domain superfamily arebelieved to induce membrane curvature. PICK1 is a distinctive protein that consists of both a BAR anda PDZ domain, and it has been associated with numerous diseases. It is known to facilitate membranecurvature during receptor-mediated endocytosis. In addition to understanding how the BAR domainfacilitates membrane curvature, it's particularly interesting to unravel the hidden links between thestructural and mechanical properties of the PICK1 BAR domain. Methods:This paper employs steered molecular dynamics (SMD) to investigate the mechanical propertiesassociated with structural changes in the PICK1 BAR domains. Results:Our findings suggest that not only do helix kinks assist in generating curvature of BAR domains,but they may also provide the additional flexibility required to initiate the binding betweenBAR domains and the membrane Conclusion:We have observed a complex interaction network within the BAR monomer and at thebinding interface of the two BAR monomers. This network is crucial for maintaining the mechanicalproperties of the BAR dimer. Owing to this interaction network, the PICK1 BAR dimer exhibits differentresponses to external forces applied in opposite directions.