Alanine Counteracts the Destabilizing Effect that Urea has on RNase-A
Rimpy K Chowhan, Fasil Ali, Mohd Y Bhat
1Department of Clinical Biochemistry, University of Kashmir, Srinagar, Jammu & Kashmir, India. tanveerali@kashmiruniversity.ac.in.
Protein and Peptide Letters
|June 21, 2016
Summary
Alanine, unlike glycine, protects proteins from urea damage. This suggests non-methylated compounds can also counteract urea
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Science
Background:
- Organisms use methylamine osmolytes to counteract urea's protein-damaging effects.
- Urea-rich cells accumulate various compounds, but non-accumulated osmolytes' protective roles are unknown.
Purpose of the Study:
- Investigate alanine's urea-counteracting properties against ribonuclease A (RNase-A) denaturation.
- Determine if non-methylamine osmolytes can offer protection against urea.
Main Methods:
- Measured thermodynamic parameters (Tm, ΔHm, ΔGD°) of RNase-A.
- Assessed RNase-A stability in the presence of alanine, urea, and glycine.
Main Results:
- Alanine demonstrated a protective effect on RNase-A stability against urea.
- Glycine did not counteract the destabilizing effects of urea on RNase-A.
Conclusions:
- Alanine may serve as an alternative osmolyte to methylamines for urea protection.
- Methylation of glycine might be evolutionarily significant for protein protection against urea.
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