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Acylphosphatase (AcP) is a small protein with 98 amino acid residues thatcatalyzes the hydrolysis of carboxyl-phosphate bonds. AcP is a typicaltwo-state protein with slow folding rate due to its relatively large contactorder in the native structure. The mechanical properties and unfolding behaviorof AcP has been studied by atomic force microscope. But the folding andunfolding dynamics at low forces has not been reported. Here using stablemagnetic tweezers, we measured the force-dependent folding rates within a forcerange from 1 pN to 3 pN, and unfolding rates from 15 pN to 40 pN. The obtainedunfolding rates show different force sensitivities at forces below and above~27 pN, which determines a free energy landscape with two energy barriers. Ourresults indicate that the free energy landscape of small globule proteins havegeneral Bactrian camel shape, and large contact order of the native stateproduces a high barrier dominate at low forces.

Free energy landscape of two-state protein Acylphosphatase with large contact order revealed by force-dependent folding and unfolding dynamics