PMID: 9532234Apr 9, 1998Paper

pH titration of native and unfolded beta-trypsin: evaluation of the delta delta G0 titration and the carboxyl pK values

Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas
A R GüntherE Rogana

Abstract

The stabilizing free energy of beta-trypsin was determined by hydrogen ion titration. In the pH range from 3.0 to 7.0, the change in free energy difference for the stabilization of the native protein relative to the unfolded one (delta delta G0 titration) was 9.51 +/- 0.06 kcal/mol. An isoelectric point of 10.0 was determined, allowing us to calculate the Tanford and Kirkwood electrostatic factor w. This factor presented a nonlinear behavior and indicated more than one type of titratable carboxyl groups in beta-trypsin. In fact, one class of carboxyl group with a pK = 3.91 +/- 0.01 and another one with a pK = 4.63 +/- 0.03 were also found by hydrogen ion titration of the protein in the folded state.

References

Feb 6, 1990·Biochemistry·D Stigter, K A Dill
Jan 1, 1972·Methods in Enzymology·Y Nozaki
Sep 14, 1993·Biochemistry·Y Huang, D W Bolen
Nov 1, 1961·Archives of Biochemistry and Biophysics·B F ERLANGERW COHEN
Nov 30, 1967·Biochemical and Biophysical Research Communications·T Chase, E Shaw

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Citations

Oct 17, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Zdeněk Perutka, Marek Šebela
Dec 11, 2003·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·E R BittarM M Santoro

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