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Updated: Mar 11, 2026

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers
Published on: July 25, 2012
Pressure acceleration of proteolysis: A general mechanism
Kazuyuki Akasaka1, Harumi Nagahata2, Akihiro Maeno2
1High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
Abstract:
Remarkable acceleration of enzymatic proteolysis by pressure at kbar range is reported with ubiquitin as substrate and α-chymotrypsin as enzyme. The acceleration is interpreted in terms of the shift of conformational equilibrium in ubiquitin from the non-degradable folded conformer to the enzyme-degradable unfolded conformer by pressure because of the lower volume of the latter, while the enzymatic activity of α-chymotrypsin is still largely retained. This mechanism is considered generally applicable to most globular proteins and the method of pressure-accelerated proteolysis will have an enormous potential utility in systems wherever efficient removal of proteins is needed.
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