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Thermal Denaturation of Collagen Analyzed by Isoconversional Method
Author(s) -
Vyazovkin Sergey,
Vincent Luc,
Sbirrazzuoli Nicolas
Publication year - 2007
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200700162
Subject(s) - chemistry , denaturation (fissile materials) , polymer chemistry , polymer science , chemical engineering , biophysics , nuclear chemistry , engineering , biology
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.

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