Influence of temperature and denaturing agents on the structural stability of calmodulin. A 1H-nuclear magnetic resonance study.
The structural stability of calmodulin was studied by 1H-nuclear magnetic resonance spectroscopy under different denaturing conditions. The presence of Ca2+ stabilizes the structural properties of the native protein. In the absence of calcium the structural integrity of calmodulin can easily be affected by elevated temperatures or by high concentrations of denaturing agents. The unfolding process under various denaturing conditions is reversible underlining the high degree of structural flexibility of this protein.
D000818:Animals; D001921:Brain; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism; D002417:Cattle; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011489:Protein Denaturation; D013696:Temperature
D002147:Calmodulin; D002118:Calcium