Biochemical and Biophysical Research Communications, Vol.291, No.4, 795-797, 2002
Linear correlation between thermal stability and folding kinetics of lysozyme
We have studied the refolding and thermal denaturation of hen egg white lysozyme in a wide range of pH values (from 1.5 to 9.4) using stopped-flow circular dichroism (CD) and differential scanning calorimetry (DSC). A linear correlation was found between the thermal denaturation temperature (T.) and the logarithm of the refolding rate of the slow folding phase of hen egg white lysozyme (Ink(2)). (C) 2002 Elsevier Science (USA).
Keywords:protein folding;pH dependence;lysozyme;stopped-flow;circular dichroism;differential scanning calorimetry