Authors: Fabrizia Foglia Paola Carullo Pompea Del Vecchio
Publish Date: 2007/10/01
Volume: 91, Issue: 1, Pages: 67-72
Abstract
The thermal stability of bovine pancreatic ribonuclease RNase A has been investigated in the presence of trimethylamine Noxide TMAO a naturally occurring osmolyte by means of differential scanning calorimetry DSC and circular dichroism CD measurements at neutral and acid pH conditions It is well known that compatible osmolytes such as TMAO are effective in stabilizing protein structure and counteracting the denaturing the effect of urea and guanidinium hydrochloride GuHCl Calorimetric results show that TMAO stabilizes RNase A at pH 70 and does not stabilize the protein at pH 40 RNase A thermal denaturation in the presence of TMAO is a reversible twostate N ⇆ D process We also show that TMAO counteracts the urea and GuHCl denaturing effect at neutral pH whereas the counteracting ability is lost at acid pH
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