Abstract
We report for the first time an atomic force microscopy (AFM) investigation of the dependence of unbinding force on temperature at controlled loading rate. AFM force measurements of biotin−avidin interactions were acquired at various temperatures ranging from 13 to 37 °C using force loading rates that are slow enough to ignore dissipative friction and to assume thermal equilibrium. With our established Poisson statistical analysis method, the unbinding force at a fixed loading rate between an individual biotin−avidin pair was extracted and was found to decrease by ∼5-fold with increasing temperature over this range. On the basis of a thermodynamic model similar to that of Bell, but developed here with additional insights, the bond stiffness, effective unbinding length, and the critical unbinding energy per biotin−avidin complex were estimated. This work takes quantitative AFM studies to the next level by allowing energies to be determined from force measurements.
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