Organic cosolvents and hen egg white lysozyme folding.
Studies on the influence of organic cosolvents on lysozyme folding have been reported. As most of the researches are confined to a few specific molecules and focus on equilibrium states, less is known about the effect on folding dynamics. We have studied the influence of six soluble organic cosolvents on hen egg white lysozyme heat induced denaturation and refolding dynamics. It was found that trifluoroethanol (TFE) can change the folding pathway significantly. With the presence of TFE, the overshot phenomenon generally observed in lysozyme folding at 222 nm disappears. The common mechanism of how organic cosolvents influence folding is analyzed. The heat induced denaturation temperature was found to have a quantitative relationship with the slow phase rate constant during folding. We discuss this finding and hypothesize that it is due to the similar influence of organic cosolvent on the transition state of heat denaturation and refolding.
Lai
B
B
State Key Laboratory for Structural Studies of Stable and Unstable Species, Institute of Physical Chemistry, College of Chemistry, Peking University, 100871, Beijing, PR China.
Cao
A
A
Lai
L
L
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D002942:Circular Dichroism; D004529:Egg White / Q000032:analysis*; D000431:Ethanol; D005260:Female; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012997:Solvents; D014270:Trifluoroethanol
D012997:Solvents; D000431:Ethanol; D014270:Trifluoroethanol; D009113:Muramidase