Chenyi An1, Wei Chen2,*
Molecular & Cellular Biomechanics, Vol.16, Suppl.2, pp. 109-110, 2019, DOI:10.32604/mcb.2019.07634
Abstract Biomembrane force probe (BFP) is a single-molecule biomechanical technique that has been widely used to characterize protein dynamics (e.g., protein-protein interactions and protein conformational changes), especially suitable for measuring force-regulated receptor-ligand binding kinetics in situ[1-4]. Integrated with various force spectroscopies, such as lifetime assay, it has become a powerful platform to systematically characterize many force-regulated receptor-ligand dissociation of great biological significance, which cannot be done with traditional solution based assays (e.g., surface plasma resonance) [5].
Even though the BFP has been quite successful in characterizing binding kinetics of weak and transient molecular interactions, it is… More >