Document Type
Article
Publication Date
7-1998
Source Publication
Biophysical Chemistry
Abstract
Using computer simulations we have studied possible effects of heating and cooling at different scan rates on unfolding and refolding of macromolecules. We have shown that even the simplest two-state reversible transition can behave irreversibly when an unfavorable combination of cooling rate, relaxation time and activation energy of refolding occurs. On the basis of this finding we suppose that apparent irreversibility of some proteins denatured by heat may result from slow relaxation on cooling rather than thermodynamic instability and/or irreversible alterations of the polypeptide chain. Using this kinetic reversible two-state model, we estimated the effects of the scan rate and kinetic parameters of the macromolecule on its unfolding–refolding process. A few recommendations are suggested on how to reach maximal possible recovery after denaturation if refolding appears to be under kinetic control.
Recommended Citation
Potekhin, Sergey A. and Kovriguine, Evgueni, "Folding Under Inequilibrium Conditions as a Possible Reason for Partial Irreversibility of Heat-Denatured Proteins: Computer Simulation Study" (1998). Chemistry Faculty Research and Publications. 242.
https://epublications.marquette.edu/chem_fac/242
Comments
Accepted version. Biophysical Chemistry, Vol. 73, No. 3 (July 1998): 241-248. DOI: © 1998 Elsevier Science B.V. Used with permission.