Striking stabilization of Rana catesbeiana ribonuclease 3 by guanidine hydrochloride.

Magali Solé, Wolfgang Brandt, Ulrich Arnold

Martin-Luther University Halle-Wittenberg, Institute of Biochemistry and Biotechnology, Kurt-Mothes Str 3, 06120 Halle, Germany.

FEBS letters 2013 Mar 18

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Unfolding by chemical denaturants and the linear extrapolation method are widely used to determine the free energy of proteins. Ribonuclease 3 from bullfrog shows an extraordinary behavior in guanidinium hydrochloride in comparison to its homologues ribonuclease A and onconase with a high transition midpoint of denaturation but an apparently low cooperativity. The analysis of the interdependence of thermal, urea-, and guanidine hydrochloride-induced unfolding revealed that whereas addition of urea resulted in the expected destabilization of all three proteins, guanidine hydrochloride acted diversely: in contrast to ribonuclease A and onconase, both of which were destabilized as expected, low concentrations of guanidine hydrochloride significantly stabilize ribonuclease 3 from bullfrog. This stabilizing effect was endorsed by in silico docking studies. Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Magali Solé, Wolfgang Brandt, Ulrich Arnold. Striking stabilization of Rana catesbeiana ribonuclease 3 by guanidine hydrochloride. FEBS letters. 2013 Mar 18;587(6):737-42