Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 33, Pages 11662-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja904462n
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Funding
- International JOINT PROJECT of the Royal Society [NIMR: U.1175.03.002.00001.04]
- MIUR [FIRB 2003]
- Medical Research Council [MC_U117584256] Funding Source: researchfish
- MRC [MC_U117584256] Funding Source: UKRI
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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 gets, with the addition of polyethylene glycol, allows easy access to subzero temperatures that might enable studies of cold denaturation of many proteins.
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