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(m)) and the logarithm of the refolding rate of the slow folding phase of hen egg white lysozyme (lnk(2)).
Cao
Aoneng
A
State Key Laboratory of Structural Chemistry for Stable and Unstable Species, Peking University, Beijing 100871, China.
Wang
Gang
G
Tang
Youqi
Y
Lai
Luhua
L
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature
C421864:hen egg lysozyme; D009113:Muramidase