title: Thermal denaturation of collagen analyzed by isoconversional method.
abstract: An isoconversional method is proposed to be used for evaluating activation energy of protein denaturation. Applied to DSC data on collagen denaturation, the method yields an activation energy that decreases throughout the process. The Lumry-Eyring model gives an explanation for this decrease and affords estimates for the enthalpy of the reversible step and the activation energy of the irreversible step of denaturation. The reversible unfolding is detectable by multi-frequency temperature-modulated DSC.
authors: Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294, USA. vyazovkin@uab.edu
authors: Sergey
authors: S
authors: Vyazovkin
authors: Luc
authors: L
authors: Vincent
authors: Nicolas
authors: N
authors: Sbirrazzuoli
mesh_terms: D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D007700:Kinetics; D011489:Protein Denaturation; D013696:Temperature; D013710:Tendons / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D003094:Collagen