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• W2063889488 abstract "A dielectric relaxation peak due to an intramolecular motion in the active site of trypsin was first observed in aqueous solution below the freezing temperature of bulk water by a time domain reflectometry method. If trypsin inhibitor is added to the solution, it vanishes. It is suggested that the motion observed is a hinge-bending deformation giving rise to the enzymatic activity of trypsin, which is prohibited by linkage of the trypsin inhibitor. Relaxation time of the motion is 3 × 102 ns at − 10°C. © 1996 John Wiley & Sons, Inc." @default.
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• W2063889488 date "1998-12-06" @default.
• W2063889488 modified "2023-09-23" @default.
• W2063889488 title "Hinge-bending deformation of enzyme observed by microwave dielectric measurement" @default.
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• W2063889488 doi "https://doi.org/10.1002/(sici)1097-0282(199608)39:2<183::aid-bip6>3.0.co;2-l" @default.
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