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. Author manuscript; available in PMC: 2017 Sep 1.
Published in final edited form as: Biochim Biophys Acta. 2016 May 24;1861(9 Pt A):1015–1024. doi: 10.1016/j.bbalip.2016.05.008

Fig. 1.

Fig. 1

Secondary structure and thermal stability of LDL fractions monitored by circular dichroism spectroscopy. Far-UV CD spectra of intact LDL(total), LDL(+), and LDL(−) (A). The melting data recorded of LDL(+) and LDL(−) at 320 nm by turbidity to monitor changes in the particle size (B) and by near-UV CD to monitor lipid re-packing upon lipoprotein disintegration and release of core lipids (C). The data were recorded using LDL samples under standard conditions (0.35 mg protein/mL, 20 mM Na phosphate buffer, pH 7.0). The melting data in panels B and C were recorded simultaneously during sample heating and cooling at a constant rate of 11 °C/h. Steep decline in CD and turbidity amplitude observed upon heating of LDL(+) above 88 °C is due to sample precipitation (D). The melting data of LDL(total) (not shown) were similar to those of LDL(+) within the error of their experimental determination.