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Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy

Peyman Obeidy1, Haoqing Wang1,2,3, Mingqin Du1, Huiqian Hu1,4, Fang Zhou1, Haoruo Zhou5, Hao Huang5, Yunduo Charles Zhao1,2, Lining Arnold Ju1,2,3


A biomembrane force probe (BFP) has recently emerged as a native-cell-surface or in situ dynamic force spectroscopy (DFS) nanotool that can measure single-molecular binding kinetics, assess mechanical properties of ligand-receptor interactions, visualize protein dynamic conformational changes and more excitingly elucidate receptor mediated cell mechanosensing mechanisms. More recently, BFP has been used to measure the spring constant of molecular bonds. This protocol describes the step-by-step procedure to perform molecular spring constant DFS analysis. Specifically, two BFP operation modes are discussed, namely the Bead-Cell and Bead-Bead modes. This protocol focuses on deriving spring constants of the molecular bond and cell from DFS raw data.

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