Article ID Journal Published Year Pages File Type
10536846 Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2012 9 Pages PDF
Abstract
► We studied the effects of pressure on deep-sea DHFR of Moritella profunda (mpDHFR). ► Enzyme activity of mpDHFR was optimal at 50 MPa. ► mpDHFR is resistant to heat but sensitive to pressure and urea. ► Volume change due to unfolding of mpDHFR is smaller than that of DHFR of E. coli. ► The cavity and surface hydration dominantly contribute to the stability of mpDHFR.
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Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
Preview
Pressure dependence of activity and stability of dihydrofolate reductases of the deep-sea bacterium Moritella profunda and Escherichia coli
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