An NMR study of the thermal stability of titin I28 in the temperature range from -16 to 65 degrees C showed that this protein can undergo cold denaturation at physiological conditions. This is the second case of a protein undergoing unbiased cold denaturation. Comparison of the stability curves in buffer and in crowded conditions shows that it is possible to measure thermodynamics parameters for unfolding even when proteins aggregate at high temperature. The use of confinement in polyacrylamide gels, with the addition of polyethylene glycol, allows easy access to subzero temperatures that might enable studies of cold denaturation of many proteins.
Cold Denaturation and Aggregation: A Comparative NMR Study of Titin I28 in Bulk and in a Confined Environment
PASTORE, ANNALISA;
2009-01-01
Abstract
An NMR study of the thermal stability of titin I28 in the temperature range from -16 to 65 degrees C showed that this protein can undergo cold denaturation at physiological conditions. This is the second case of a protein undergoing unbiased cold denaturation. Comparison of the stability curves in buffer and in crowded conditions shows that it is possible to measure thermodynamics parameters for unfolding even when proteins aggregate at high temperature. The use of confinement in polyacrylamide gels, with the addition of polyethylene glycol, allows easy access to subzero temperatures that might enable studies of cold denaturation of many proteins.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
