| Literature DB >> 10852311 |
Abstract
A large number of thermodynamic data including the free energy, enthalpy, entropy, and heat capacity changes were collected for the denaturation of various proteins. Regression indicated that remarkable enthalpy-entropy compensation occurred in protein unfolding, which meant that the change in enthalpy was almost compensated by a corresponding change in entropy resulting in a smaller net free energy change. This behavior was proposed to result from the water molecule reorganization, which contributed significantly to the enthalpy and entropy changes but little to the free energy change in protein unfolding. It turned out that the enthalpy-entropy compensation could provide novel insights into the problem of enthalpy and entropy convergence in protein unfolding.Entities:
Mesh:
Substances:
Year: 2000 PMID: 10852311 DOI: 10.1016/s0301-4622(00)00130-7
Source DB: PubMed Journal: Biophys Chem ISSN: 0301-4622 Impact factor: 2.352