Cold denaturation and aggregation: a comparative NMR study of titin I28 in bulk and in a confined environment.
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.
Sanfelice
Domenico
D
Department of Chemistry, Università di Napoli Federico II, via Cinthia, 80126 Napoli, Italy.
Tancredi
Teodorico
T
Politou
Anastasia
A
Pastore
Annalisa
A
Temussi
Piero A
PA
D000180:Acrylic Resins / Q000494:pharmacology; D003080:Cold Temperature; D064211:Connectin; D009682:Magnetic Resonance Spectroscopy; D009124:Muscle Proteins / Q000737:chemistry* / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism*; D055550:Protein Stability; D013816:Thermodynamics; D000099166:Polyacrylamides
D000180:Acrylic Resins; D064211:Connectin; D009124:Muscle Proteins; D011092:Polyethylene Glycols; D011494:Protein Kinases; D000099166:Polyacrylamides