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On the conformational instability of human serum low-density lipoprotein: effect of temperature
Abstract:
When examined by circular dichroism and ultraviolet spectroscopy, human serum low-density lipoprotein (LDL) and its delipidated product, apo LDL, exhibited reversible thermal changes. The more marked temperature sensitivity of apo LDL as compared to LDL was taken to support a constraining role by lipids on the observed structural instability of the apoprotein.