title: Cold denaturation and aggregation: a comparative NMR study of titin I28 in bulk and in a confined environment.
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.
authors: Department of Chemistry, Università di Napoli Federico II, via Cinthia, 80126 Napoli, Italy.
authors: Domenico
authors: D
authors: Sanfelice
authors: Teodorico
authors: T
authors: Tancredi
authors: Anastasia
authors: A
authors: Politou
authors: Annalisa
authors: A
authors: Pastore
authors: Piero A
authors: PA
authors: Temussi
mesh_terms: 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
chemical_list: D000180:Acrylic Resins; D064211:Connectin; D009124:Muscle Proteins; D011092:Polyethylene Glycols; D011494:Protein Kinases; D000099166:Polyacrylamides