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) a...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2002-03, Vol.291 (4), p.795-797
Main Authors: Cao, Aoneng, Wang, Gang, Tang, Youqi, Lai, Luhua
Format: Article
Language:English
Subjects:
Animals
Calorimetry, Differential Scanning
Circular Dichroism
differential scanning calorimetry
Enzyme Stability
Hydrogen-Ion Concentration
Kinetics
lysozyme
Muramidase - chemistry
pH dependence
Protein Denaturation
Protein Folding
stopped-flow
Temperature
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Summary: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).
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2002.6526