Peptide hydrogen exchange rates in Streptomyces subtilisin inhibitor.

Biochimica Et Biophysica Acta
K AkasakaS Murao

Abstract

The exchange reaction of the peptide NH protons of a microbial protease inhibitor (Streptomyces subtilisin inhibitor) with deuterium atoms in 2H2O (p2H 6.8) has been studied by proton magnetic resonance in the temperature range 56-71 degrees C. Both slowly and rapidly exchanging processes have been observed. The number of slowly exchanging protons is estimated to be 25 +/- 2 per subunit of the protein molecule. The decay of the slowly exchanging proton signals follows a single time-exponential function at each temperature. The observed first-order rate constants have been analyzed to give the denaturated fraction of the protein as a function of temperature with a consequent enthalpy (56 kcal/mol) and an entropy (137 cal/degree per mol) of denaturation. The results indicate the high conformational stability of this protein against heat denaturation.

References

Dec 23, 1974·Biochemical and Biophysical Research Communications·H L CrespiU H Smith
Sep 28, 1972·Journal of Molecular Biology·M NakanishiA Ikegami
Jul 15, 1973·Journal of Molecular Biology·H TakesadaM Tsuboi
Apr 25, 1973·Journal of Molecular Biology·M NakanishiA Ikegami
Mar 14, 1972·Journal of Molecular Biology·M NakanishiM Kanehisa

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